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AB60835

Recombinant human PIM1 protein

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(2 Publications)

Recombinant human PIM1 protein is a Human Full Length protein, expressed in Baculovirus infected Sf9 cells, with >90%, suitable for SDS-PAGE, FuncS.

View Alternative Names

Serine/threonine-protein kinase pim-1, PIM1

4 Images
Functional Studies - Recombinant human PIM1 protein (AB60835)
  • FuncS

Unknown

Functional Studies - Recombinant human PIM1 protein (AB60835)

The specific activity of PIM1 (ab60835) was determined to be 270 nmol/min/mg as per activity assay protocol

Functional Studies - Recombinant human PIM1 protein (AB60835)
  • FuncS

Unknown

Functional Studies - Recombinant human PIM1 protein (AB60835)

Sample Kinase Activity Plot.

SDS-PAGE - Recombinant human PIM1 protein (AB60835)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant human PIM1 protein (AB60835)

ab60835 on SDS-PAGE, MW ~62kDa.

SDS-PAGE - Recombinant human PIM1 protein (AB60835)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant human PIM1 protein (AB60835)

SDS PAGE analysis of ab60835

Key facts

Purity

>90% SDS-PAGE

Expression system

Baculovirus infected Sf9 cells

Tags

GST tag N-Terminus

Applications

FuncS, SDS-PAGE

applications

Biologically active

Yes

Biological activity

Active

Accession

P11309

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.5 Constituents: 25% Glycerol (glycerin, glycerine), 0.87% Sodium chloride, 0.79% Tris HCl, 0.00385% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.0038% EGTA, 0.00292% EDTA, 0.00174% PMSF

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Product details

ab204880 (RPS6 peptide) can be utilized as a substrate for assessing kinase activity

Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P11309","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
True

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The PIM1 protein also known as Proto-oncogene serine/threonine-protein kinase Pim-1 is a serine/threonine kinase with a mass of approximately 44 kDa. PIM1 is expressed ubiquitously in the body but shows higher expression levels in hematopoietic tissues such as spleen thymus and bone marrow. Within the cell PIM1 predominantly locates to the cytoplasm but can also be found in the nucleus. The PIM1 protein contains conserved kinase domains which are essential for its catalytic activity.
Biological function summary

PIM1 protein plays an important role in cell survival proliferation and differentiation. It functions as a regulator within signal transduction pathways and although not forming part of a larger complex its kinase activity affects other proteins' phosphorylation status influencing various cellular processes. High levels of PIM1 expression are often associated with increased cellular proliferation and are involved in feedback loops enhancing cell survival.

Pathways

PIM1 protein contributes significantly to the JAK/STAT and PI3K/AKT signaling pathways which are important for the regulation of immune responses and cell growth. Within these pathways PIM1 interacts with other proteins such as STAT5 and AKT mediating signals that promote cell cycle progression and apoptosis inhibition. Its role is particularly important for the modulation of hematopoietic and immune functions where it facilitates cellular responses to external growth stimuli.

PIM1 protein is implicated in several cancers notably hematological malignancies like leukemia and lymphomas. The overexpression of PIM1 cooperates with oncogenes like MYC and BCL2 contributing to tumorigenesis by promoting uncontrolled cell proliferation and survival. Additionally PIM1 is under investigation for its role in cardiovascular diseases where it may impact cardiomyocyte survival and heart repair mechanisms. Targeting PIM1 and its associated pathways may offer therapeutic potentials in these conditions.

Specifications

Form

Liquid

Additional notes

Purity: >90% as determined by densitometry. Affinity purified.

General info

Function

Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis (PubMed : 15528381, PubMed : 1825810, PubMed : 31548394). Exerts its oncogenic activity through : the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3) (PubMed : 18593906). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity (By similarity). The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis (By similarity). Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1 (By similarity). Phosphorylation of MAP3K5, another proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis (PubMed : 19749799). Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C (PubMed : 16356754). Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability (PubMed : 12431783). Promotes cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels (PubMed : 18593906). Phosphorylation of CDKN1B, induces 14-3-3 proteins binding, nuclear export and proteasome-dependent degradation (PubMed : 18593906). May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3 (PubMed : 10664448). Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis (By similarity). Acts as a positive regulator of mTORC1 signaling by mediating phosphorylation and inhibition of DEPDC5 component of the GATOR1 complex (PubMed : 31548394). Acts as a negative regulator of innate immunity by mediating phosphorylation and inactivation of GBP1 in absence of infection : phosphorylation of GBP1 induces interaction with 14-3-3 protein sigma (SFN) and retention in the cytosol (PubMed : 37797010). Also phosphorylates and activates the ATP-binding cassette transporter ABCG2, allowing resistance to drugs through their excretion from cells (PubMed : 18056989). Promotes brown adipocyte differentiation (By similarity).

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. PIM subfamily.

Post-translational modifications

Autophosphorylated on both serine/threonine and tyrosine residues. Phosphorylated. Interaction with PPP2CA promotes dephosphorylation.. Ubiquitinated, leading to proteasomal degradation.

Subcellular localisation

Nucleus

Product protocols

Target data

Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis (PubMed : 15528381, PubMed : 1825810, PubMed : 31548394). Exerts its oncogenic activity through : the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3) (PubMed : 18593906). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity (By similarity). The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis (By similarity). Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1 (By similarity). Phosphorylation of MAP3K5, another proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis (PubMed : 19749799). Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C (PubMed : 16356754). Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability (PubMed : 12431783). Promotes cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels (PubMed : 18593906). Phosphorylation of CDKN1B, induces 14-3-3 proteins binding, nuclear export and proteasome-dependent degradation (PubMed : 18593906). May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3 (PubMed : 10664448). Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis (By similarity). Acts as a positive regulator of mTORC1 signaling by mediating phosphorylation and inhibition of DEPDC5 component of the GATOR1 complex (PubMed : 31548394). Acts as a negative regulator of innate immunity by mediating phosphorylation and inactivation of GBP1 in absence of infection : phosphorylation of GBP1 induces interaction with 14-3-3 protein sigma (SFN) and retention in the cytosol (PubMed : 37797010). Also phosphorylates and activates the ATP-binding cassette transporter ABCG2, allowing resistance to drugs through their excretion from cells (PubMed : 18056989). Promotes brown adipocyte differentiation (By similarity).
See full target information PIM1

Publications (2)

Recent publications for all applications. Explore the full list and refine your search

Communications biology 4:1221 PubMed34697370

2021

PIM1 phosphorylation of the androgen receptor and 14-3-3 ζ regulates gene transcription in prostate cancer.

Applications

Unspecified application

Species

Unspecified reactive species

Sophie E Ruff,Nikita Vasilyev,Evgeny Nudler,Susan K Logan,Michael J Garabedian

Arteriosclerosis, thrombosis, and vascular biology 40:783-801 PubMed31969012

2020

PIM1 (Moloney Murine Leukemia Provirus Integration Site) Inhibition Decreases the Nonhomologous End-Joining DNA Damage Repair Signaling Pathway in Pulmonary Hypertension.

Applications

Unspecified application

Species

Unspecified reactive species

Marie-Claude Lampron,Géraldine Vitry,Valérie Nadeau,Yann Grobs,Renée Paradis,Nolwenn Samson,Ève Tremblay,Olivier Boucherat,Jolyane Meloche,Sébastien Bonnet,Steeve Provencher,François Potus,Roxane Paulin
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