Invitrogen

HSC70 Polyclonal Antibody

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Datasheet
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Datasheet
Protocols
Questions & Answers
HSC70 Polyclonal Antibody

Product Details

PA5-96133

Applications
Tested Dilution
Publications

Western Blot (WB)

1:500-1:1,000
-

Immunohistochemistry (Paraffin) (IHC (P))

1:50-1:200
-

Immunocytochemistry (ICC/IF)

1:50-1:200
-

ELISA (ELISA)

1 µg/mL
-
Product Specifications

Species Reactivity

Human, Mouse, Non-human primate, Rat

Host/Isotype

Rabbit / IgG

Class

Polyclonal

Type

Antibody

Immunogen

Recombinant fusion protein containing a sequence corresponding to amino acids 510-615 of human Hsc70/HSPA8 (NP_0065881)
View immunogen

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Liquid

Concentration

3.07 mg/mL

Purification

Affinity Chromatography

Storage buffer

PBS, pH 7.3, with 50% glycerol

Contains

0.09% sodium azide

Storage conditions

-20°C, Avoid Freeze/Thaw Cycles

Shipping conditions

Wet ice

RRID

AB_2807935

Product Specific Information

Immunogen sequence: LSKEDIERMV QEAEKYKAED EKQRDKVSSK NSLESYAFNM KATVEDEKLQ GKINDEDKQK ILDKCNEIIN WLDKNQTAEK EEFEHQQKEL EKVCNPIITK LYQSAG

Positive Samples: Cellular Location: Cell membrane, Cytoplasm, Melanosome, Nucleus, nucleolus

Target Information

The HSP70 family is a set of highly conserved proteins that are induced by a variety of biological stresses, including heat stress, in every organism in which the proteins have been examined. The human HSP70 family members include: HSP70, a protein which is strongly inducible in all organisms but which is also constitutively expressed in primate cells; HSP72, a 72 kDa protein that is induced exclusively under stress conditions; HSC70, or cognate protein, is a 72 kDa, constitutively expressed, protein which is involved in the uncoating of clathrin coated vesicles; GRP78, or BiP, is a glucose regulated 78 kDa protein localized in the endoplasmic reticulum; and p75, or HSP75, a 75 kDa protein that is found within the mitochondria. HSC70 (also known as HSC71, HSC73, HSP73, p72, prp73) is expressed constitutively and is slightly heat-inducible. HSC70 binds to the exposed loop of clathrin light chains to promote uncoating and can also bind the cytoskeleton which may facilitate cytoskeletal rearrangements. HSC70 has been shown to stimulate lysosomal degradation of intracellular proteins and to retard both aggregation and folding of mitochondrial precursor proteins in vitro.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.

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Bioinformatics

Protein Aliases: AAG2; constitutive heat shock protein 70; epididymis luminal protein 33; epididymis secretory sperm binding protein Li 72p; FAM10A1; Heat shock 70 kDa protein 8; heat shock 70kd protein 10; heat shock 70kD protein 8; heat shock 70kDa protein 8; Heat shock cognate 71 kDa protein; heat shock cognate hsc73; heat shock cognate protein 54; Heat shock cognate protein 70; heat shock protein 8; heat shock protein A8; heat shock protein cognate 70; Heat shock protein family A member 8; HIP; LAP; LAP-1; Lipopolysaccharide-associated protein 1; LPS-associated protein 1; MGC131511; MGC29929; N-myristoyltransferase inhibitor protein 71; Protein FAM10A1; SNC6

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Gene Aliases: 2410008N15Rik; HEL-33; HEL-S-72p; HSC54; HSC70; HSC71; Hsc73; HSP71; HSP73; HSPA10; HSPA8; LAP-1; LAP1; NIP71

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UniProt ID: (Human) P11142, (Rat) P63018, (Mouse) P63017

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Entrez Gene ID: (Human) 3312, (Rat) 24468, (Mouse) 15481

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Function(s)
G-protein coupled receptor binding phosphatidylserine binding protein binding ATP binding ATPase activity enzyme binding MHC class II protein complex binding heat shock protein binding ubiquitin protein ligase binding ATPase activity, coupled poly(A) RNA binding unfolded protein binding C3HC4-type RING finger domain binding cadherin binding involved in cell-cell adhesion receptor binding ADP binding nucleotide binding
Process(es)
transcription, DNA-templated mRNA processing protein folding RNA splicing protein refolding negative regulation of transcription, DNA-templated positive regulation of mRNA splicing, via spliceosome chaperone mediated protein folding requiring cofactor regulation of cell cycle chaperone-mediated protein folding clathrin coat disassembly negative regulation of fibril organization mRNA splicing, via spliceosome protein targeting to lysosome response to unfolded protein neurotransmitter secretion cellular response to starvation viral process regulation of protein stability regulation of protein complex assembly regulation of mRNA stability ATP metabolic process regulation of protein complex stability chaperone-mediated autophagy late endosomal microautophagy protein targeting to lysosome involved in chaperone-mediated autophagy chaperone-mediated protein transport involved in chaperone-mediated autophagy cell-cell adhesion regulation of cellular response to heat regulation of protein import chaperone-mediated autophagy translocation complex disassembly regulation of transcription, DNA-templated
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