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AB167924

Recombinant Human PSAP protein

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(1 Review)

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(1 Publication)

Recombinant Human PSAP protein is a Human Full Length protein, in the 17 to 524 aa range, expressed in HEK 293 cells, with >95%, < 1 EU/µg endotoxin level, suitable for ELISA, WB, Mass Spec, SDS-PAGE.

View Alternative Names

GLBA, SAP1, PSAP, Prosaposin, Proactivator polypeptide

1 Images
SDS-PAGE - Recombinant Human PSAP protein (AB167924)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human PSAP protein (AB167924)

12% SDS-PAGE analysis of ab167924 Lane 1 : reduced and boiled sample, 2.5μg/lane
Lane 2 : non-reduced and non-boiled sample, 2.5μg/lane

The ~66 kDa band corresponds to whole PSAP (prosaposin) molecule that consists of four saposin units. The individual saposins naturally cleave off the prosaposin which results in ~15, ~35 and ~50 kDa fragments of mono-, di- and trisaposins, respectively.

Key facts

Purity

>95% Densitometry

Endotoxin level

< 1 EU/µg

Expression system

HEK 293 cells

Tags

His tag C-Terminus

Applications

ELISA, SDS-PAGE, Mass Spec, WB

applications

Biologically active

No

Accession

P07602

Animal free

No

Carrier free

No

Species

Human

Reconstitution

Reconstitute in 200 µL of water

Storage buffer

Constituents: 99% Phosphate Buffer, 0.43% Sodium chloride

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p>ab167924 migrates at ~ 65 kDa, and at ~ 25 kDa (disaposins)or ~ 35 kDa (trisaposins) on SDS-PAGE.</p>" } } }

Sequence info

[{"sequence":"ASGPVLGLKECTRGSAVWCQNVKTASDCGAVKHCLQTVWNKPTVKSLPCDICKDVVTAAGDMLKDNATEEEILVYLEKTCDWLPKPNMSASCKEIVDSYLPVILDIIKGEMSRPGEVCSALNLCESLQKHLAELNHQKQLESNKIPELDMTEVVAPFMANIPLLLYPQDGPRSKPQPKDNGDVCQDCIQMVTDIQTAVRTNSTFVQALVEHVKEECDRLGPGMADICKNYISQYSEIAIQMMMHMQPKEICALVGFCDEVKEMPMQTLVPAKVASKNVIPALELVEPIKKHEVPAKSDVYCEVCEFLVKEVTKLIDNNKTEKEILDAFDKMCSKLPKSLSEECQEVVDTYGSSILSILLEEVSPELVCSMLHLCSGTRLPALTVHVTQPKDGGFCEVCKKLVGYLDRNLEKNSTKQEILAALEKGCSFLPDPYQKQCDQFVAEYEPVLIEILVEVMDPSFVCLKIGACPSAHKPLLGTEKCIWGPSYWCQNTETAAQCNAVEHCKRHVWNKLHHHHHH","proteinLength":"Full Length","predictedMolecularWeight":"57.7 kDa","actualMolecularWeight":null,"aminoAcidEnd":524,"aminoAcidStart":17,"nature":"Recombinant","expressionSystem":"HEK 293 cells","accessionNumber":"P07602","tags":[{"tag":"His","terminus":"C-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate long-term storage conditions
-80°C
False

Specifications

Form

Lyophilized

Additional notes

ab167924 was purifed using Ni-NTA chromatography.

General info

Function

Saposin-A and saposin-C stimulate the hydrolysis of glucosylceramide by beta-glucosylceramidase (EC 3.2.1.45) and galactosylceramide by beta-galactosylceramidase (EC 3.2.1.46). Saposin-C apparently acts by combining with the enzyme and acidic lipid to form an activated complex, rather than by solubilizing the substrate.. Saposin-B stimulates the hydrolysis of galacto-cerebroside sulfate by arylsulfatase A (EC 3.1.6.8), GM1 gangliosides by beta-galactosidase (EC 3.2.1.23) and globotriaosylceramide by alpha-galactosidase A (EC 3.2.1.22). Saposin-B forms a solubilizing complex with the substrates of the sphingolipid hydrolases.. Saposin-D is a specific sphingomyelin phosphodiesterase activator (EC 3.1.4.12).. Prosaposin. Behaves as a myelinotrophic and neurotrophic factor, these effects are mediated by its G-protein-coupled receptors, GPR37 and GPR37L1, undergoing ligand-mediated internalization followed by ERK phosphorylation signaling.. Saposins are specific low-molecular mass non-enzymic proteins, they participate in the lysosomal degradation of sphingolipids, which takes place by the sequential action of specific hydrolases.

Post-translational modifications

The lysosomal precursor is proteolytically processed to 4 small peptides, which are similar to each other and are sphingolipid hydrolase activator proteins.. N-linked glycans show a high degree of microheterogeneity.. The one residue extended Saposin-B-Val is only found in 5% of the chains.

Product protocols

Target data

Saposin-A and saposin-C stimulate the hydrolysis of glucosylceramide by beta-glucosylceramidase (EC 3.2.1.45) and galactosylceramide by beta-galactosylceramidase (EC 3.2.1.46). Saposin-C apparently acts by combining with the enzyme and acidic lipid to form an activated complex, rather than by solubilizing the substrate.. Saposin-B stimulates the hydrolysis of galacto-cerebroside sulfate by arylsulfatase A (EC 3.1.6.8), GM1 gangliosides by beta-galactosidase (EC 3.2.1.23) and globotriaosylceramide by alpha-galactosidase A (EC 3.2.1.22). Saposin-B forms a solubilizing complex with the substrates of the sphingolipid hydrolases.. Saposin-D is a specific sphingomyelin phosphodiesterase activator (EC 3.1.4.12).. Prosaposin. Behaves as a myelinotrophic and neurotrophic factor, these effects are mediated by its G-protein-coupled receptors, GPR37 and GPR37L1, undergoing ligand-mediated internalization followed by ERK phosphorylation signaling.. Saposins are specific low-molecular mass non-enzymic proteins, they participate in the lysosomal degradation of sphingolipids, which takes place by the sequential action of specific hydrolases.
See full target information PSAP

Publications (1)

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

Cell 184:4651-4668.e25 PubMed34450028

2021

Rescue of a lysosomal storage disorder caused by Grn loss of function with a brain penetrant progranulin biologic.

Applications

Unspecified application

Species

Unspecified reactive species

Todd Logan,Matthew J Simon,Anil Rana,Gerald M Cherf,Ankita Srivastava,Sonnet S Davis,Ray Lieh Yoon Low,Chi-Lu Chiu,Meng Fang,Fen Huang,Akhil Bhalla,Ceyda Llapashtica,Rachel Prorok,Michelle E Pizzo,Meredith E K Calvert,Elizabeth W Sun,Jennifer Hsiao-Nakamoto,Yashas Rajendra,Katrina W Lexa,Devendra B Srivastava,Bettina van Lengerich,Junhua Wang,Yaneth Robles-Colmenares,Do Jin Kim,Joseph Duque,Melina Lenser,Timothy K Earr,Hoang Nguyen,Roni Chau,Buyankhishig Tsogtbaatar,Ritesh Ravi,Lukas L Skuja,Hilda Solanoy,Howard J Rosen,Bradley F Boeve,Adam L Boxer,Hilary W Heuer,Mark S Dennis,Mihalis S Kariolis,Kathryn M Monroe,Laralynne Przybyla,Pascal E Sanchez,Rene Meisner,Dolores Diaz,Kirk R Henne,Ryan J Watts,Anastasia G Henry,Kannan Gunasekaran,Giuseppe Astarita,Jung H Suh,Joseph W Lewcock,Sarah L DeVos,Gilbert Di Paolo
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