Recombinant Rabbit Anti-HSPA8 Antibody (clone R07-1B7) (CAT#: VS3-FY710)

• Immunogen
• Synthetic peptide of human Hsc70.

• Host Species
• Rabbit

• Type
• Rabbit IgG

• Specificity
• Human, Mouse, Rat, Hamster HSPA8

• Species Reactivity
• Human, Mouse, Rat, Hamster

• Clone
• R07-1B7

• Applications
• Western Blot, Immunohistochemistry-Paraffin, Immunoprecipitation

• Conjugate
• Unconjugated

• MW
• Calculated MW: 71 kDa; Observed MW: 71 kDa

• Purification
• Affinity Purified

• Purity
• >95% as determined by SDS-PAGE

• Buffer
• 50 mM Tris-Glycine, pH 7.4, 0.15 M NaCl, 40% glycerol, 0.05% BSA

• Preservative
• 0.01% Sodium azide

• Storage
• Centrifuge briefly prior to opening vial. Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

• Application Notes
• Western Blot: 1/500-1/1000
  Immunohistochemistry-Paraffin: 1/50-1/100
  Immunoprecipitation: 1/20

• Alternative Names
• Heat Shock Protein Family A (Hsp70) Member 8; Lipopolysaccharide-Associated Protein 1; Heat Shock 70kDa Protein 8; LPS-Associated Protein 1; HSPA10; HSC70; HSP73; LAP-1; Epididymis Secretory Sperm Binding Protein Li 72p; N-Myristoyltransferase Inhibitor Protein 71; Constitutive Heat Shock Protein 70; Heat Shock Cognate 71 KDa Protein; Epididymis Luminal Protein 33

• Gene ID
• 3312

• UniProt ID
• P11142

• Sequence Similarities
• Belongs to the heat shock protein 70 family.

• Cellular Localization
• Cell membrane, Cytoplasm, Membrane, Nucleus, Spliceosome

• Post Translation Modifications
• Acetylated.
  ISGylated.
  Trimethylation at Lys-561 reduces fibrillar SNCA binding.

• Protein Refseq
• NP_006588.1; NP_694881.1

• Function
• Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488).
  This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488, PubMed:12526792).
  The co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488, PubMed:12526792).
  The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1 (PubMed:24318877, PubMed:27474739, PubMed:24121476, PubMed:26865365).
  Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70 (PubMed:12526792).
  Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:10722728, PubMed:11276205).
  Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1 (PubMed:23990462).
  Interacts with VGF-derived peptide TLQP-21 (PubMed:28934328).

Secondary Antibody

• 2ND-054CQ
• Goat Anti-Rabbit IgG Antibody, R-PE

• 2ND-055CQ
• Chicken Anti-Rabbit IgG (H&L) Antibody

• 2ND-057CQ
• Donkey Anti-Rabbit IgG (H&L) Antibody

• 2ND-059CQ
• Goat Anti-Rabbit IgG (H&L) Antibody

• 2ND-060CQ
• Llama Anti-Rabbit IgG (H&L) Antibody

• 2ND-061CQ
• Sheep Anti-Rabbit IgG (H&L) Antibody

Isotype Control

• MOB-208CQ
• Rabbit IgG Isotype Control Antibody