Anti-Hsp90 alpha Monoclonal Antibody | MyBioSource MBS190539 product information

product summary

company name :

MyBioSource

product type :

antibody

product name :

Anti-Hsp90 alpha Monoclonal Antibody

catalog :

MBS190539

quantity :

0.1 mg

price :

260 USD

clonality :

monoclonal

host :

mouse

conjugate :

nonconjugated

clone name :

2G5.G3

reactivity :

human, mouse, rat

application :

western blot, ELISA, immunohistochemistry, immunocytochemistry

more info or order :

MyBioSource product webpage

product information

catalog number :

MBS190539

products type :

Antibody

products full name :

Anti-Hsp90 alpha Monoclonal Antibody

products short name :

Hsp90 alpha

other names :

heat shock protein HSP 90-alpha isoform 2; Heat shock protein HSP 90-alpha; heat shock protein HSP 90-alpha; HSP 86; heat shock 86 kDa; heat shock 90kD protein 1, alpha; heat shock 90kDa protein 1, alpha; renal carcinoma antigen NY-REN-38; heat shock 90kD protein, alpha-like 4; heat shock 90kD protein 1, alpha-like 4; heat shock protein 90kDa alpha (cytosolic), class A member 1; Heat shock 86 kDa; HSP 86; HSP86; Renal carcinoma antigen NY-REN-38

products gene name :

Hsp90 alpha

other gene names :

HSP90AA1; HSP90AA1; HSPN; LAP2; HSP86; HSPC1; HSPCA; Hsp89; Hsp90; HSP89A; HSP90A; HSP90N; HSPCAL1; HSPCAL4; FLJ31884; HSP90A; HSPC1; HSPCA

uniprot entry name :

HS90A_HUMAN

clonality :

Monoclonal

isotype :

IgG1

clone :

2G5.G3

host :

Mouse

reactivity :

Human, mouse, rat

specificity :

Hsp90 alpha. This antibody recognizes human, mouse, and rat Hsp90alpha. Other species have not been tested. It does not crossreact with Hsp90beta in ELISA.

form :

100ug Protein G-purified antibody in PBS, pH 7.4.

storage stability :

This antibody is stable for at least one (1) year at -20 degree C. Avoid repeated freezing and thawing.

tested application :

ELISA; Immunoblot; Immunohistochemistry; Immunocytochemistry

app notes :

Immunoblotting: use at 0.5-1ug/ml. A band of ~90 kDa is detected. ELISA Immunohistochemistry/ Immunocytochemistry Imunoprecipitation. User should determine optimal concentrations for their application. Positive control: HeLa cell lysate.

other info1 :

Antigen: Human Hsp90 alpha. Preservative: None.

other info2 :

Dilution Instructions: Dilute in PBS or medium which is identical to that used in the assay system.

products description :

Hsp90 is an abundantly and ubiquitously expressed heat shock protein found in all eukaryotic cells. It exists in two principal forms, alpha and beta, which share 85% sequence homology. Both forms are expressed in the cytosol. Hsp90alpha exists primarily as a homodimer while Hsp90beta exists mainly as a monomer. Hsp90 plays a role in folding, assembly, maturation, and stabilization of specific proteins as a key component of a chaperone complex. Most of the Hsp90-regulated proteins that have been identified are involved in cell signaling; kinases, v-Src, Wee1, c-Raf, and p53 are some examples. When bound to ATP, Hsp90 interacts with cochaperones Cdc37, p23, and various immunophilin-like proteins to form complexes that stabilize and protect target proteins from proteasomal degradation.

ncbi gi num :

154146191

ncbi acc num :

NP_005339.3

ncbi gb acc num :

NM_005348.3

uniprot acc num :

P07900

ncbi mol weight :

84,660 Da

ncbi pathways :

Antigen Processing And Presentation Pathway 83074!!Antigen Processing And Presentation Pathway 485!!Axon Guidance Pathway 105688!!Cell Cycle, Mitotic Pathway 105765!!Centrosome Maturation Pathway 105807!!Class I PI3K Signaling Events Pathway 138022!!Class I PI3K Signaling Events Mediated By Akt Pathway 138020!!EBV LMP1 Signaling Pathway 198790!!ErbB Receptor Signaling Network Pathway 138016!!G2/M Transition Pathway 105801

ncbi summary :

HSP90 proteins are highly conserved molecular chaperones that have key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90 proteins normally associate with other cochaperones and play important roles in folding newly synthesized proteins or stabilizing and refolding denatured proteins after stress. There are 2 major cytosolic HSP90 proteins, HSP90AA1, an inducible form, and HSP90AB1 (MIM 140572), a constitutive form. Other HSP90 proteins are found in endoplasmic reticulum (HSP90B1; MIM 191175) and mitochondria (TRAP1; MIM 606219) (Chen et al., 2005 [PubMed 16269234]).[supplied by OMIM]

uniprot summary :

Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Ref.15 Ref.21. Subunit structure: Homodimer. Interacts with AHSA1, FNIP1, HSF1, SMYD3 and TOM34. Interacts with TERT; the interaction, together with PTGES3, is required for correct assembly and stabilization of the TERT holoenzyme complex. Interacts with CHORDC1 and DNAJC7. Interacts with STUB1 and UBE2N; may couple the chaperone and ubiquitination systems. Ref.17 Ref.18 Ref.19 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.32 Ref.45 Ref.46. Subcellular location: Cytoplasm. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.30. Domain: The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins like the co-chaperone STUB1. Post-translational modification: ISGylated. Ref.27S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1. Sequence similarities: Belongs to the heat shock protein 90 family.

size :

0.1 mg

price :

260 USD

more info or order :

MyBioSource product webpage