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AB9702

Recombinant human PDGF AA protein

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(3 Publications)

Recombinant human PDGF AA protein is a Human Full Length protein, expressed in Escherichia coli, with >98%, suitable for SDS-PAGE, FuncS.

View Alternative Names

PDGF1, PDGFA, Platelet-derived growth factor subunit A, PDGF subunit A, PDGF-1, Platelet-derived growth factor A chain, Platelet-derived growth factor alpha polypeptide

Key facts

Purity

>98% SDS-PAGE

Expression system

Escherichia coli

Tags

Tag free

Applications

FuncS, SDS-PAGE

applications

Biologically active

Yes

Biological activity

Active

Accession

P04085

Animal free

No

Carrier free

No

Species

Human

Storage buffer

Constituents: 0.06% Acetic acid

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

The biological activity is determined by the dose-dependent stimulation of the proliferation of BALB/c 3T3 cells, is < 1.0 ng/ml, corresponding to a specific activity of > 1 x 106 units/mg

Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":"24 kDa","actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P04085","tags":[]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°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.

Platelet-derived growth factor AA or PDGF-AA is a member of the PDGF protein family which is involved in various cellular processes. The PDGF-AA protein has a molecular mass of approximately 24 kDa. It is expressed in a wide range of tissues including fibroblasts smooth muscle cells and neurons. The protein is considered a homodimer composed of two A chains and it plays an important role in cell signaling by binding to PDGF receptors on the surface of target cells.
Biological function summary

PDGF-AA influences cell proliferation migration and differentiation. It acts as a mitogen especially for mesenchymal cells such as fibroblasts and smooth muscle cells. PDGF-AA is often part of a signaling complex where it activates PDGF receptor-alpha (PDGFR-α) leading to autophosphorylation and subsequent activation of downstream effectors. This strengthens tissue development and wound healing processes.

Pathways

PDGF-AA integrates into critical signaling pathways like the PI3K/AKT pathway and the MAPK/ERK pathway. These pathways regulate cell growth and survival. PDGF-AA binds specifically to PDGFR-α which shares importance with other PDGF isoforms such as PDGF-BB in orchestrating cellular responses through similar pathways thereby ensuring precise physiological outcomes.

PDGF-AA is implicated in conditions like cancer and fibrosis. Aberrant signaling involving PDGF-AA can lead to unchecked cell proliferation contributing to tumorigenesis. Similarly PDGF-AA is connected to fibrotic diseases where excessive tissue scarring occurs due to overactive fibroblast stimulation. PDGF-BB another member of the PDGF protein family often gets studied alongside PDGF-AA for their combined roles in these pathological states.

Specifications

Form

Lyophilized

Additional notes

Sterile filtered Greater than 98% pure by HPLC analyses. Endotoxin level is less than 0.1 ng per g (1EU/g).

General info

Function

Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal lung alveolar septum formation during embryogenesis, normal development of the gastrointestinal tract, normal development of Leydig cells and spermatogenesis. Required for normal oligodendrocyte development and normal myelination in the spinal cord and cerebellum. Plays an important role in wound healing. Signaling is modulated by the formation of heterodimers with PDGFB (By similarity).

Sequence similarities

Belongs to the PDGF/VEGF growth factor family.

Product protocols

Target data

Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal lung alveolar septum formation during embryogenesis, normal development of the gastrointestinal tract, normal development of Leydig cells and spermatogenesis. Required for normal oligodendrocyte development and normal myelination in the spinal cord and cerebellum. Plays an important role in wound healing. Signaling is modulated by the formation of heterodimers with PDGFB (By similarity).
See full target information PDGFA

Publications (3)

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

Biochemical and biophysical research communications 530:252-258 PubMed32828295

2020

An immortalized human adipose-derived stem cell line with highly enhanced chondrogenic properties.

Applications

Unspecified application

Species

Unspecified reactive species

Dakota B Katz,Nguyen P T Huynh,Alireza Savadipour,Ilan Palte,Farshid Guilak

Inflammatory bowel diseases 26:524-533 PubMed31750910

2019

miR-29a-5p/STAT3 Positive Feedback Loop Regulates TETs in Colitis-Associated Colorectal Cancer.

Applications

Unspecified application

Species

Unspecified reactive species

Aiping Wang,Song Deng,Xi Chen,Chang Yu,Qun Du,Yanli Wu,Gang Chen,Ling Hu,Chenxia Hu,Yanwu Li

Nature communications 10:1455 PubMed30926783

2019

Ventral tegmental area astrocytes orchestrate avoidance and approach behavior.

Applications

Unspecified application

Species

Unspecified reactive species

J A Gomez,J M Perkins,G M Beaudoin,N B Cook,S A Quraishi,E A Szoeke,K Thangamani,C W Tschumi,M J Wanat,A M Maroof,M J Beckstead,P A Rosenberg,C A Paladini
View all publications

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