Anti-HSP90AB1 antibody (1-300)

Clonality:	Polyclonal
Conjugation:	Unconjugated
Isotype:	IgG
Formulation:	PBS with 0.01% Thimerosal, 50% Glycerol, pH7.3.
Purification:	Affinity purification
Dilution Range:	WB 1:500-1:2000 IF/ICC 1:50-1:200
Storage Instruction:	Store at-20°C for up to 1 year from the date of receipt, and avoid repeat freeze-thaw cycles.

Gene Symbol:	HSP90AB1
Gene ID:	3326
Uniprot ID:	HS90B_HUMAN
Immunogen Region:	1-300
Immunogen:	Recombinant fusion protein containing a sequence corresponding to amino acids 1-300 of human Hsp90 Beta (NP_031381.2).
Immunogen Sequence:	MPEEVHHGEEEVETFAFQAE IAQLMSLIINTFYSNKEIFL RELISNASDALDKIRYESLT DPSKLDSGKELKIDIIPNPQ ERTLTLVDTGIGMTKADLIN NLGTIAKSGTKAFMEALQAG ADISMIGQFGVGFYSAYLVA EKVVVITKHNDDEQYAWESS AGGSFTVRADHGEPIGRGTK VILHLKEDQTEYLEERRVKE VVKKHSQFIGYPITLYLEKE REKEISDDEAEEEKGEKEE

Post Translational Modifications	Ubiquitinated in the presence of STUB1-UBE2D1 complex (in vitro). ISGylated. S-nitrosylated.negatively regulates the ATPase activity. Phosphorylation at Tyr-301 by SRC is induced by lipopolysaccharide. Phosphorylation at Ser-226 and Ser-255 inhibits AHR interaction. Methylated by SMYD2.facilitates dimerization and chaperone complex formation.promotes cancer cell proliferation. Cleaved following oxidative stress resulting in HSP90AB1 protein radicals formation.disrupts the chaperoning function and the degradation of its client proteins.
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 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. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle. Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. They first alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression. Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation. Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery. Main chaperone involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription. Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1.the translocation process is mediated by the cargo receptor TMED10. (Microbial infection) Binding to N.meningitidis NadA stimulates monocytes. Seems to interfere with N.meningitidis NadA-mediated invasion of human cells (Probable).
Protein Name	Heat Shock Protein Hsp 90-Beta Hsp 90 Heat Shock 84 Kda Hsp 84 Hsp84
Database Links	Reactome: R-HSA-168928 Reactome: R-HSA-2029482 Reactome: R-HSA-3371497 Reactome: R-HSA-3371511 Reactome: R-HSA-3371568 Reactome: R-HSA-3371571 Reactome: R-HSA-399954 Reactome: R-HSA-5336415 Reactome: R-HSA-6798695 Reactome: R-HSA-844456 Reactome: R-HSA-8852276 Reactome: R-HSA-8937144 Reactome: R-HSA-8939211 Reactome: R-HSA-9013418 Reactome: R-HSA-9018519 Reactome: R-HSA-9613829 Reactome: R-HSA-9660826 Reactome: R-HSA-9679191 Reactome: R-HSA-9705671
Cellular Localisation	Cytoplasm Melanosome Nucleus Secreted Cell Membrane Dynein Axonemal Particle Cell Surface Identified By Mass Spectrometry In Melanosome Fractions From Stage I To Stage Iv Translocates With Birc2 From The Nucleus To The Cytoplasm During Differentiation Secreted When Associated With Tgfb1 Processed Form (Lap)
Alternative Antibody Names	Anti-Heat Shock Protein Hsp 90-Beta antibody Anti-Hsp 90 antibody Anti-Heat Shock 84 Kda antibody Anti-Hsp 84 antibody Anti-Hsp84 antibody Anti-HSP90AB1 antibody Anti-HSP90B antibody Anti-HSPC2 antibody Anti-HSPCB antibody

Information sourced from Uniprot.org

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