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Recombinant Human AP-3 complex subunit beta-1 (AP3B1), partial

Recombinant Human AP-3 complex subunit beta-1 (AP3B1), partial

Code
MSDS	MSDS Datasheet
Size	Pls inquire
Source
Conjugate
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Product Details
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Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

AP3B1

Uniprot NO.

O00203

Alternative Names

Adapter related protein complex 3 beta 1 subunit; Adapter-related protein complex 3 subunit beta-1; Adaptor protein complex AP-3 subunit beta-1; Adaptor protein complex AP3 beta1 subunit; ADTB3; ADTB3A; AP-3 complex subunit beta-1; AP3 complex beta1 subunit; AP3B1; AP3B1_HUMAN; Beta-3A-adaptin; Beta3A adaptin; Clathrin assembly protein complex 3 beta 1 large chain; Clathrin assembly protein complex 3 beta-1 large chain; HPS; PE

Species

Homo sapiens (Human)

Source

Yeast

Expression Region

1-1094

Target Protein Sequence

MSSNSFPYNE QSGGGEATEL GQEATSTISP SGAFGLFSSD LKKNEDLKQM LESNKDSAKL DAMKRIVGMI AKGKNASELF PAVVKNVASK NIEIKKLVYV YLVRYAEEQQ DLALLSISTF QRALKDPNQL IRASALRVLS SIRVPIIVPI MMLAIKEASA DLSPYVRKNA AHAIQKLYSL DPEQKEMLIE VIEKLLKDKS TLVAGSVVMA FEEVCPDRID LIHKNYRKLC NLLVDVEEWG QVVIIHMLTR YARTQFVSPW KEGDELEDNG KNFYESDDDQ KEKTDKKKKP YTMDPDHRLL IRNTKPLLQS RNAAVVMAVA QLYWHISPKS EAGIISKSLV RLLRSNREVQ YIVLQNIATM SIQRKGMFEP YLKSFYVRST DPTMIKTLKL EILTNLANEA NISTLLREFQ TYVKSQDKQF AAATIQTIGR CATNILEVTD TCLNGLVCLL SNRDEIVVAE SVVVIKKLLQ MQPAQHGEII KHMAKLLDSI TVPVARASIL WLIGENCERV PKIAPDVLRK MAKSFTSEDD LVKLQILNLG AKLYLTNSKQ TKLLTQYILN LGKYDQNYDI RDRTRFIRQL IVPNVKSGAL SKYAKKIFLA QKPAPLLESP FKDRDHFQLG TLSHTLNIKA TGYLELSNWP EVAPDPSVRN VEVIELAKEW TPAGKAKQEN SAKKFYSESE EEEDSSDSSS DSESESGSES GEQGESGEEG DSNEDSSEDS SSEQDSESGR ESGLENKRTA KRNSKAKGKS DSEDGEKENE KSKTSDSSND ESSSIEDSSS DSESESEPES ESESRRVTKE KEKKTKQDRT PLTKDVSLLD LDDFNPVSTP VALPTPALSP SLMADLEGLH LSTSSSVISV STPAFVPTKT HVLLHRMSGK GLAAHYFFPR QPCIFGDKMV SIQITLNNTT DRKIENIHIG EKKLPIGMKM HVFNPIDSLE PEGSITVSMG IDFCDSTQTA SFQLCTKDDC FNVNIQPPVG ELLLPVAMSE KDFKKEQGVL TGMNETSAVI IAAPQNFTPS VIFQKVVNVA NVGAVPSGQD NIHRFAAKTV HSGSLMLVTV ELKEGSTAQL IINTEKTVIG SVLLRELKPV LSQG
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Protein Length

Partial

Tag Info

N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Storage Condition

Store at -20°C, for extended storage, conserve at -20°C or -80°C.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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Target Background

Function(From Uniprot)

Subunit of non-clathrin- and clathrin-associated adaptor protein complex 3 (AP-3) that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. AP-3 appears to be involved in the sorting of a subset of transmembrane proteins targeted to lysosomes and lysosome-related organelles. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals.

Gene References into Functions

point mutation c.2702C>G in exon 23 of the AP3B1 gene caused deletion of 112 bp in the mRNA in two siblings. This mutation activates a cryptic donor splice site that overrules the wild-type donor splice site of this exon. Three other novel mutations in AP3B1 were identified, that is, a nonsense mutation c.716G>A (p.Trp239Ter), a 1-bp and a 4-bp deletion c.177delA and c.1839_1842delTAGA, respectively PMID:28585318
Synergistic defects of UNC13D and AP3B1 leading to adult hemophagocytic lymphohistiocytosis. PMID:25980904
Using a co-affinity purification strategy, authors have identified the beta subunit of the AP-3 adapter protein complex, AP3B1, as a binding partner for the M proteins of the zoonotic paramyxoviruses Nipah virus and Hendra virus. PMID:25210190
Data indicate that RUN and FYVE domain protein Rabip4'(RUFY1) interacts specifically and directly with adaptor protein complex AP-3. PMID:23144738
The study provides a description of two unrelated individuals with Hermansky Pudlak syndrome type 2 associated with novel mutations in AP3B1. PMID:19679886
diphosphoinositol pentakisphosphate-mediated pyrophosphorylation of AP3B1 modulates the interaction with Kif3A and, as a consequence, affects the release of HIV-1 virus-like particles. PMID:19934039
Two nonsense mutations in ADTB3A, C1578T (R-->X) and G2028T (E-->X), result in lack of ADTB3A mRNA and beta3A protein production and a severe, G-CSF-responsive neutropenia in addition to oculocutaneous albinism and platelet storage pool deficiency. PMID:11809908
Description of mutations in HPS genes that cause Hermansky-Pudlak syndrome (review) PMID:12125811
We defined a homozygous genomic deletion in AP3B1, the gene encoding the beta chain of the adaptor protein-3 (AP-3) complex. The mutation leads to in-frame skipping of exon 15 and thus perturbs proper assembly of the heterotetrameric AP-3 complex. PMID:16537806
A novel homozygous mutation in AP3B1 was detected in a 2-year-old patient with oculocutaneous albinism and immunodeficiency with Hermansky-Pudlak syndrome type II and eventual acute fatal hemophagocytic lymphohistiocytosis. PMID:16551969
Mutations in AP3B1 is not associated with familial hemophagocytic lymphohistiocytosis PMID:18000860
AP-1 and AP-3 are involved in the formation of distinct types of clathrin-coated vesicles, each of which is characterized by the incorporation of specific cargo membrane proteins PMID:18410487
Experimental investigation of five specific genes, AP3B1, ATP6AP1, BLOC1S1, LAMP2, and RAB11A, has confirmed novel roles for these proteins in the proper initiation of macroautophagy in amino acid-starved fibroblasts. PMID:19246570