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Search results

1000 results found for “Glypican”

Name

Description

Product #

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  • View Data Sheet

    Name :

    CDC37 Human, His

    Description:

    Cell Division Cycle 37 Human Recombinant, His Tag

    Cell Division Cycle 37 homolog, P50CDC37, CDC37, Hsp90 chaperone protein kinase-targeting subunit, CDC37 cell division cycle 37 homolog, hsp90 co-chaperone Cdc37, CDC37A.

    Product # :

    PRO-140

    Price :

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    Shipping Method :

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    Shipped at Room temp

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    • source
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    • More Info

    Description

    CDC37, His Protein is a 45.71 kDa protein containing 388 amino acids fused to a 10 aa N-Terminal His-tag.

    Source

    E. coli

    Formulation

    CDC37, His Human was filtered (0.4µm) and lyophilized from 0.5mg/ml supplied in
    20mM TRIS, 50mM NaCl, pH 7.5.

    More Info

    • Introduction

      CDC37, His protein is extremely parallel to Cdc 37, a cell division cycle control protein of Sacchromyces cerevisiae. CDC37 is a molecular chaperone with a detailed role in cell signal transduction. CDC37 forms a complex with Hsp90 and several protein kinases including CDK4, CDK6, SRC, RAF-1, MOK, and eIF2 alpha kinases CDC37 has a vital part in directing Hsp90 to its target kinases.

    • Synonyms

      Cell Division Cycle 37 homolog, P50CDC37, CDC37, Hsp90 chaperone protein kinase-targeting subunit, CDC37 cell division cycle 37 homolog, hsp90 co-chaperone Cdc37, CDC37A.

    • Stability

      Store lyophilized CDC37 His human at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted CDC37 can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      Add deionized water to prepare a working stock solution of 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL DRGCRECKRK VAECQRKLKE LEVAEGGKAE LERLQAEAQQ LRKEERSWEQ KLEEMRKKEK SMPWNVDTLS KDGFSKSMVN TKPEKTEEDS EEVREQKHKT FVEKYEKQIK HFGMLRRWDD SQKYLSDNVH LVCEETANYL VIWCIDLEVE EKCALMEQVA HQTIVMQFIL ELAKSLKVDP RACFRQFFTK IKTADRQYME GFNDELEAFK ERVRGRAKLR IEKAMKEYEE EERKKRLGPG GLDPVEVYES LPEELQKCFD VKDVQMLQDA ISKMDPTDAK YHMQRCIDSG LWVPNSKASE AKEGEEAGPG DPLLEAVPKT GDEKDVSV

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Cdc37 His Human
  • View Data Sheet

    Name :

    ULBP2 Human, Sf9

    Description:

    UL16 Binding Protein 2 Human Recombinant, Sf9

    ULBP2, ALCAN-alpha, N2DL2, NKG2DL2, RAET1H, UL16 Binding Protein 2, Retinoic Acid Early Transcript 1H, UL16-Binding Protein 2, ALCAN-Alpha, NKG2D Ligand 2, N2DL-2.

    Product # :

    PRO-2378

    Price :

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    Description

    ULBP2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 200 amino acids (26-216a.a) and having a molecular mass of 22.7kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). ULBP2 is fused to a 9 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ULBP2 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      ULBP2 is a member of the MHC class I family. ULBP2 is ligand for the NKG2D receptor, composed with at least ULBP1 and ULBP3. ULBPs promote multiple signaling pathways in primary NK cells, triggering the production of cytokines and chemokines. Binding of ULBPs ligands to NKG2D encourages calcium mobilization and activation of the JAK2, STAT5, ERK and PI3K kinase/Akt signal transduction pathway. In CMV infected cells, ULBP2 cooperates with soluble CMV glycoprotein UL16. This cooperation is blocked with the NKG2D receptor, providing a mechanism in which CMV infected cells can escape the immune system. Additionally, UL16 causes ULBP2 to be held in the ER and cis-Golgi apparatus so that it does not reach the cell surface.

    • Synonyms

      ULBP2, ALCAN-alpha, N2DL2, NKG2DL2, RAET1H, UL16 Binding Protein 2, Retinoic Acid Early Transcript 1H, UL16-Binding Protein 2, ALCAN-Alpha, NKG2D Ligand 2, N2DL-2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      ADPGRADPHS LCYDITVIPK FRPGPRWCAV QGQVDEKTFL HYDCGNKTVT PVSPLGKKLN VTTAWKAQNP VLREVVDILT EQLRDIQLEN YTPKEPLTLQ ARMSCEQKAE GHSSGSWQFS FDGQIFLLFD SEKRMWTTVH PGARKMKEKW ENDKVVAMSF HYFSMGDCIG WLEDFLMGMD STLEPSAGAP LAMSHHHHHH.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Ulbp2 Human Sf9
  • View Data Sheet

    Name :

    ULBP3 Human

    Description:

    UL16 Binding Protein 3 Human Recombinant

    UL16 Binding Protein 3, Retinoic Acid Early Transcript 1N, ALCAN-Gamma, NKG2DL3, N2DL-3, RAET1N, UL16-Binding Protein 3, NKG2D Ligand 3, N2DL3, ULBP3.

    Product # :

    PRO-2039

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

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    Description

    ULBP3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Asp30-Gly217) containing 198 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 23.25kDa.

    Source

    Escherichia Coli.

    Formulation

    ULBP3 was filtered (0.4 µm) and lyophilized in 20mM Tris buffer, 50mM NaCl and 0.1% v/v amisoft CS-22, pH 7.5.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      UL16 Binding Protein 3 (ULBP3) is a ligand for the NKG2D receptor in NK cells. ULBPs activate different signaling pathways resulting in the production of cytokines and chemokines. ULBP3 is a ligand for the KLRK1/NKG2D receptor, along with at least ULBP1 and ULBP2. Binding of ULBPs ligands to KLRK1/NKG2D stimulates calcium mobilization and activation of the JAK2, STAT5, ERK and PI3K kinase/Akt signal transduction pathway. ULBP3 has lower affinity for KLRK1/NKG2D compared to ULBP1 and ULBP2 and stimulates weaker signaling responses than does ULBP2 or ULBP1.

    • Synonyms

      UL16 Binding Protein 3, Retinoic Acid Early Transcript 1N, ALCAN-Gamma, NKG2DL3, N2DL-3, RAET1N, UL16-Binding Protein 3, NKG2D Ligand 3, N2DL3, ULBP3.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. ULBP3 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASDAHSLWYNFT IIHLPRHGQQ WCEVQSQVDQ KNFLSYDCGS DKVLSMGHLE EQLYATDAWG KQLEMLREVG QRLRLELADT ELEDFTPSGP LTLQVRMSCE CEADGYIRGS WQFSFDGRKF LLFDSNNRKW TVVHAGARRM KEKWEKDSGL TTFFKMVSMR DCKSWLRDFL MHRKKRLEPT APPTMAPG.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Ulbp3 Human
  • View Data Sheet

    Name :

    CRYAB Human, His

    Description:

    Crystallin Alpha B Human Recombinant, His Tag

    CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.

    Product # :

    HSP-088

    Price :

    Quantity :

    Shipping Method :

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    • description
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    Description

    CRYAB Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (1-175) and having a molecular mass of 21.2kDa. CRYAB is fused to an 8 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CRYAB solution (1mg/ml) contains 10% glycerol & Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Synonyms

      CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPT STSLSPFYLR PPSFLRAPSW FDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR KYRIPADVDP LTITSSLSSD GVLTVNGPRK QVSGPERTIP ITREEKPAVT AAPKKLEHHH HHH.

    • Background

      Alpha-B crystallin (CRYAB), a small heat shock protein, stands as a multifaceted molecular chaperone integral to cellular homeostasis and stress response. In its human recombinant form, CRYAB becomes a focal point in biomedical research, offering a controlled platform to explore its structural intricacies, cellular functions, and potential therapeutic applications. This research embarks on a comprehensive journey to unveil the diverse roles of CRYAB Human Recombinant, shedding light on its structural attributes, cellular interactions, and its implications in health and disease. By delving into the properties of CRYAB, scientists aim to deepen our understanding of cellular proteostasis and explore novel avenues in the treatment of protein misfolding disorders.

      Structural Insights into CRYAB Human Recombinant:

      CRYAB, forming oligomeric complexes, possesses a dynamic structural configuration crucial for its chaperone function. The human recombinant form, designed for controlled study, provides a unique window into the three-dimensional intricacies of CRYAB. Understanding its structure is fundamental for deciphering how CRYAB engages with client proteins, preventing their aggregation and maintaining cellular proteostasis.

      Cellular Functions in Proteostasis:

      As a molecular chaperone, CRYAB plays a pivotal role in preserving cellular proteostasis by preventing the aggregation of misfolded proteins. Beyond its chaperone function, CRYAB is implicated in diverse cellular processes, including modulation of apoptosis, regulation of cytoskeletal dynamics, and participation in cell signaling pathways. Elucidating the multifaceted functions of CRYAB Human Recombinant provides insights into its roles in health and disease.

      Implications in Neurodegenerative Disorders:

      CRYAB has garnered attention in the context of neurodegenerative disorders, where protein misfolding and aggregation are central pathological features. Studies involving CRYAB Human Recombinant have revealed its neuroprotective properties, suggesting its potential as a therapeutic target for conditions like Alzheimer's and Parkinson's diseases. Understanding the mechanisms by which CRYAB mitigates protein aggregation in neuronal cells holds promise for developing targeted interventions.

      CRYAB in Cardiovascular Health:

      The chaperone function of CRYAB extends to the cardiovascular system, where it safeguards against protein aggregation in cardiomyocytes. CRYAB Human Recombinant studies have illuminated its protective role in cardiac tissues, positioning it as a potential therapeutic avenue for heart diseases characterized by protein misfolding.

      Challenges and Future Directions:

      While the potential of CRYAB Human Recombinant in therapeutics is evident, challenges persist. Fine-tuning its applications, understanding its interactions with diverse client proteins, and exploring the intricacies of its roles in different cellular contexts are critical for translational success. Additionally, deciphering the specific mechanisms by which CRYAB contributes to the alleviation of protein misfolding disorders remains an active area of investigation.

      CRYAB Human Recombinant emerges as a linchpin in the cellular orchestra, orchestrating a symphony of functions vital for proteostasis. Its structural insights, diverse cellular functions, and therapeutic implications position it at the forefront of biomedical research. As researchers continue to unravel the molecular nuances of CRYAB, they not only deepen our understanding of cellular proteostasis but also pave the way for innovative treatments in neurodegenerative and cardiovascular disorders, shaping the future of precision medicine and protein folding therapeutics.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Cryab Human His
  • View Data Sheet

    Name :

    EDAR Human

    Description:

    Ectodysplasin A Receptor Human Recombinant

    Ectodysplasin A Receptor, DL, Ectodysplasin 1, Anhidrotic Receptor, Anhidrotic Ectodysplasin Receptor 1, Ectodermal Dysplasia Receptor, Ectodysplasin-A Receptor, Downless Homolog, EDA-A1 Receptor, ECTD10A, ECTD10B, EDA3, HRM1, ED3, Tumor Necrosis Factor Receptor Superfamily Member EDAR, Downless, Mouse, Homolog Of, EDA-A1R, EDA1R, ED1R, ED5, Tumor necrosis factor receptor superfamily member EDAR.

    Product # :

    PRO-2092

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    Description

    EDAR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 445 amino acids (27-448 a.a) and having a molecular mass of 48.2kDa. EDAR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    EDAR protein solution (0.25mg/ml) containing 20mM Tris-HCl (pH 8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ectodysplasin A Receptor, also known as EDAR belongs to the tumor necrosis factor receptor family. EDAR is a receptor for the soluble ligand ectodysplasin A, and is capable of activating the nuclear factor-kappaB, JNK, as well as caspase-independent cell death pathways. EDAR is necessary for the development of hair, teeth, and other ectodermal derivatives. Furthermore, mutations in EDAR resulted in autosomal dominant and recessive forms of hypohidrotic ectodermal dysplasia.

    • Synonyms

      Ectodysplasin A Receptor, DL, Ectodysplasin 1, Anhidrotic Receptor, Anhidrotic Ectodysplasin Receptor 1, Ectodermal Dysplasia Receptor, Ectodysplasin-A Receptor, Downless Homolog, EDA-A1 Receptor, ECTD10A, ECTD10B, EDA3, HRM1, ED3, Tumor Necrosis Factor Receptor Superfamily Member EDAR, Downless, Mouse, Homolog Of, EDA-A1R, EDA1R, ED1R, ED5, Tumor necrosis factor receptor superfamily member EDAR.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSEYSNCGE NEYYNQTTGL CQECPPCGPG EEPYLSCGYG TKDEDYGCVP CPAEKFSKGG YQICRRHKDC EGFFRATVLT PGDMENDAEC GPCLPGYYML ENRPRNIYGM VCYSCLLAPP NTKECVGATS GASANFPGTS GSSTLSPFQH AHKELSGQGH LATALIIAMS TIFIMAIAIV LIIMFYILKT KPSAPACCTS HPGKSVEAQV SKDEEKKEAP DNVVMFSEKD EFEKLTATPA KPTKSENDAS SENEQLLSRS VDSDEEPAPD KQGSPELCLL SLVHLAREKS ATSNKSAGIQ SRRKKILDVY ANVCGVVEGL SPTELPFDCL EKTSRMLSST YNSEKAVVKT WRHLAESFGL KRDEIGGMTD GMQLFDRIST AGYSIPELLT KLVQIERLDA VESLCADILE WAGVVPPASQ PHAAS.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Edar Human
  • View Data Sheet

    Name :

    BIRC7 Human

    Description:

    Baculoviral IAP Repeat-Containing 7 Human Recombinant

    Baculoviral IAP repeat-containing protein 7, KIAP, MLIAP, RNF50, ML-IAP, LIVIN, Kidney inhibitor of apoptosis protein, Melanoma inhibitor of apoptosis protein, RING finger protein 50, BIRC7.

    Product # :

    PRO-612

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    Description

    BIRC7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 318 amino acids (1-298 a.a.) and having a molecular mass of 34kDa. BIRC7 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BIRC7 protein solution (1mg/ml) containing 20mM Tris pH-8, 1mM DTT, 0.1M NaCl, 2mM EDTA and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      BIRC7 is a part of the inhibitor of apoptosis protein (IAP) family and contains a single copy of a baculovirus IAP repeat (BIR) as well as a RING-type zinc finger domain. The BIR domain is necessary for inhibitory activity & cooperates with caspases, while the RING finger domain sometimes increases anti-apoptotic activity but doesn’t inhibit apoptosis by itself. 2 transcript variants encoding diverse isoforms have been found for this gene. The 2 isoforms have dissimilar antiapoptotic characteristics, with isoform a protecting cells from apoptosis induced by staurosporine and isoform b defending cells from apoptosis. BIRC7 has direct contact with several caspases together with caspase-3, caspase-7, & caspase –9. BIRC7 inhibits the activation of caspase-9 induced by Apaf-1, cytochrome c, and dATP.

    • Synonyms

      Baculoviral IAP repeat-containing protein 7, KIAP, MLIAP, RNF50, ML-IAP, LIVIN, Kidney inhibitor of apoptosis protein, Melanoma inhibitor of apoptosis protein, RING finger protein 50, BIRC7.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGPKDSAKCL HRGPQPSHWA AGDGPTQERC GPRSLGSPVL GLDTCRAWDH VDGQILGQLR PLTEEEEEEG AGATLSRGPA FPGMGSEELRLASFYDWPLT AEVPPELLAA AGFFHTGHQD KVRCFFCYGG LQSWKRGDDP WTEHAKWFPS CQFLLRSKGR DFVHSVQETH SQLLGSWDPW EEPEDAAPVA PSVPASGYPE LPTPRREVQS ESAQEPGGVS PAEAQRAWWV LEPPGARDVE AQLRRLQEER TCKVCLDRAV SIVFVPCGHL VCAECAPGLQ LCPICRAPVR SRVRTFLS.

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    Birc7 Human
  • View Data Sheet

    Name :

    CACYBP Human

    Description:

    Calcyclin Binding Protein Human Recombinant

    S100A6BP, S100A6 Binding Protein, GIG5, PNAS-107, RP1-102G20.6, SIP, CACYBP, hCacyBP, Siah-interacting protein, MGC87971.

    Product # :

    PRO-831

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    Description

    CACYBP Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 205 amino acids (1-185a.a.) and having a molecular mass of 23.4 kDa. CACYBP protein is fused to a 20 amino acid His tag at N-terminus and is purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    CACYBP Human solution containing 20mM Tris HCL pH-8, 1mM DTT, 0.1M NaCl & 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      CACYBP (calcyclin binding protein) participates in calcium-dependent ubiquitination and subsequent proteosomal degradation of target proteins. CACYBP acts as a molecular bridge in ubiquitin E3 complexes. CACYBP is involved in the ubiquitin-mediated degradation of beta-catenin.

    • Synonyms

      S100A6BP, S100A6 Binding Protein, GIG5, PNAS-107, RP1-102G20.6, SIP, CACYBP, hCacyBP, Siah-interacting protein, MGC87971.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MQQKSQKKAE LLDNEKPAAV VAPITTGYTV KISNYGWDQS DKFVKIYITL TGVHQVPTEN VQVHFTERSF DLLVKNLNGK SYSMIVNNLL KPISVEGSSK KVKTDTVLIL CRKKVENTRW DYLTQVEKEC KEKEKPSYDT ETDPSEGLMN VLKKIYEDGD DDMKRTINKA WVESREKQAK GDTEF.

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    Cacybp Human
  • View Data Sheet

    Name :

    YWHAG Human

    Description:

    Tyr-3/Trp-5 Monooxygenase Activation Protein Gamma Human Recombinant

    14-3-3 protein gamma, Protein kinase C inhibitor protein 1, KCIP-1, YWHAG, Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, gamma polypeptide.

    Product # :

    PKA-238

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    Description

    YWHAG Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 247 amino acids (1-247) and having a molecular mass of 28 kDa. YWHAG is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    YWHAG solution containing 20mM Tris 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms that have been identified in mammals. The 14-3-3gamma, a subtype of the 14-3-3 family of proteins, was thought to be brain and neuron-specific. It has been shown to interact with RAF1 and protein kinase C, proteins involved in various signal transduction pathways.

    • Synonyms

      14-3-3 protein gamma, Protein kinase C inhibitor protein 1, KCIP-1, YWHAG, Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, gamma polypeptide.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MVDREQLVQK ARLAEQAERY DDMAAAMKNV TELNEPLSNE ERNLLSVAYK NVVGARRSSW RVISSIEQKT SADGNEKKIE MVRAYREKIE KELEAVCQDV LSLLDNYLIK NCSETQYESK VFYLKMKGDY YRYLAEVATG EKRATVVESS EKAYSEAHEI SKEHMQPTHP IRLGLALNYS VFYYEIQNAP EQACHLAKTA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDD DGGEGNN.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Ywhag Human
  • View Data Sheet

    Name :

    CRYAB Mouse

    Description:

    Crystallin Alpha B Mouse Recombinant

    CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.

    Product # :

    HSP-018

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    Description

    Recombinant CRYAB Mouse produced in E.Coli is a single, non-glycosylated polypeptide chain containing 175 amino acids and having a molecular mass of 20 kDa. Mouse CRYAB is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Mouse CRYAB protein solution contains 20mM Tris-HCl buffer pH-8 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      Alpha crystallins are composed of two gene products ; alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20). They act as molecular chaperones and hold them in in large soluble aggregates. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional function of a-crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-B is expressed widely in many tissues and organs and occurs in many neurological diseases.

    • Synonyms

      CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFST ATSLSPFYLR PPSFLRAPSW IDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR KYRIPADVDP LTITSSLSSD GVLTVNGPRK QVSGPERTIP ITREEKPAVA AAPKK.

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    Cryab Mouse
  • View Data Sheet

    Name :

    ANGPT1 Human

    Description:

    Angiopoietin-1 Human Recombinant

    Angiopoietin 1, KIAA0003, ANG-1, AGP1, AGPT.

    Product # :

    CYT-074

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    • sds-page

    Description

    ANGPT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 480 amino acids (20-498) and having a molecular mass of 55.6 kDa.The ANGPT1 is purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ANGPT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1M Urea and 5% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    sds-page

    ANGPT1-sds-page - Product image 1

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    • Introduction

      ANGPT1 is an angiogenic factor which intervenes in blood vessel maturation and takes part in endothelial development. ANGPT1 is a secreted ligand for Tie-2, a cell surface receptor tyrosine kinase expressed in endothelial and hemopoietic cells. The glycosylated ANGPT1 protein has a coiled-coil region in the amino terminus and a fibrinogen-like domain at the carboxy terminus.

    • Synonyms

      Angiopoietin 1, KIAA0003, ANG-1, AGP1, AGPT.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MSNQRRSPEN SGRRYNRIQH GQCAYTFILP EHDGNCREST TDQYNTNALQ RDAPHVEPDF SSQKLQHLEH VMENYTQWLQ KLENYIVENM KSEMAQIQQN AVQNHTATML EIGTSLLSQT AEQTRKLTDV ETQVLNQTSR LEIQLLENSL STYKLEKQLL QQTNEILKIH EKNSLLEHKI LEMEGKHKEE LDTLKEEKEN LQGLVTRQTY IIQELEKQLN RATTNNSVLQ KQQLELMDTV HNLVNLCTKE GVLLKGGKRE EEKPFRDCAD VYQAGFNKSG IYTIYINNMP EPKKVFCNMD VNGGGWTVIQ HREDGSLDFQ RGWKEYKMGF GNPSGEYWLG NEFIFAITSQ RQYMLRIELM DWEGNRAYSQ YDRFHIGNEK QNYRLYLKGH TGTAGKQSSL ILHGADFSTK DADNDNCMCK CALMLTGGWW FDACGPSNLN GMFYTAGQNH GKLNGIKWHY FKGPSYSLRS TTMMIRPLDF

    • Background

      This factor was found in the conditioned medium of the human neuroepithelioma cell line SHEP1 and the mouse myoblast cell line C2C12ras. The cDNA encoding a protein of 498 amino acids was isolated by using a secretion-trap expression cloning procedure exploiting the presence of a signal sequence present in growth factors that are secreted by producer cells (Davis et al, 1996). Murine and human factors show 97 % identity at the amino acid level. For a related factor see: CDT6. The human gene has been mapped to chromosome 8q22.3-q23 (Cheung et al, 1998).

      The expression of angiopoietin-1 mRNA is downregulated by PDGF, EGF, IL1-beta, and TGF-beta (Enholm et al, 1997).

      Angiopoietin-1 is a ligand for the receptor-like tyrosine kinase designated TIE-2 (Davis et al, 1996). Binding of Angiopoietin-1 to its receptor induces tyrosine phosphorylation of the cytoplasmic receptor domain. A naturally occuring antagonist of Angiopoietin-1 binding to TIE-2 is Angiopoietin-2. Angiopoietin-1 also binds to the TIE-1 receptor and this interaction appears to be critical for the development of the right-hand side venous system. It is dispensable for the left-hand side venous system, suggesting that right-hand and left-hand side vascular networks are established early before asymmetrical features of the network become morphologically discernible Loughna and Sato, 2001).

      Angiopoietin-1 does not directly promote the growth of cultured endothelial cells. Angiopoietin-1 is chemotactic for endothelial cells (Witzenbichler et al, 1998). Excess soluble TIE-2 receptors abolish the chemotactic response of endothelial cells toward angiopoietin-1. Angiopoietin-1 has been shown to counteract cell death by apoptosis in cultured endothelial cells (Holash et al, 1999). Angiopoietin-1 also acts as an apoptosis survival factor for endothelial cells and this effect is augmented by the presence of VEGF (Kwak et al, 1999).

      Angiopoietin-2 dose-dependently blocks directed migration toward Angiopoietin-1. Carlson et al (2001) have shown that Ang-1 binds rather selectively to vitronectin and that Ang-1 can directly support adhesion of human umbilical vein endothelial cells and fibroblasts in a process mediated by integrins.

      The physiologic roles of Angiopoietin-1 and its receptor are limited to angiogenic processes that occur subsequent to the earlier vasculogenic and angiogenic actions of the VEGF family and their receptors. However, it is unlike most of the known angiogenesis factors such as VEGF and other classical endothelial cell growth factors in that addition of the factor to cultures of endothelial cells does not directly promote cell growth even though the TIE-2 receptor becomes activated. Angiopoietin-1 also appears to be incapable of inducing the formation of tubules by endothelial cells.

      Angiopoietins can potentiate the effects of other angiogenic cytokines. An investigation of the impact of angiopoietins on neovascularization in vivo in the cornea micropocket assay of neovascularization demonstrates that neither Angiopoietin-1 nor Angiopoietin-2 alone promote neovascularization. Holash et al (1999) have shown that a subset of tumors initially grows by coopting existing host vessels. Regression of these vessels via a process that involves disruption of interactions between endothelial cells and smooth muscle cells as well as cell death by apoptosis of endothelial cells first causes loss of tumour cells before angiogenesis begins at the tumor margin and the tumor is rescued under the influence of VEGF, Angiopoietin-1, and probably other angiogenic stimuli.

      The embryonic expression pattern of Angiopoietin-1 suggests that it plays a particularly important role in the developing heart. Angiopoietin-1 is expressed highly in the myocardial wall surrounding the endocardium expressing TIE-2. Expression of Angiopoietin-1 becomes much more widespread later in development.

      ANGPT1 Protein has a total Mw of 55.6kDa.

      What is the source or expression system of ANGPT1 Protein?
      Escherichia Coli.

      What is the Purity of ANGPT1 Protein?
      ANGPT1 Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of ANGPT1 Protein?
      The biological functionality of ANGPT1 Protein will be determined in the future.

      What is the amino acid sequence of ANGPT1 Protein?
      MSNQRRSPEN SGRRYNRIQH GQCAYTFILP EHDGNCREST TDQYNTNALQ RDAPHVEPDF SSQKLQHLEH VMENYTQWLQ KLENYIVENM KSEMAQIQQN AVQNHTATML EIGTSLLSQT AEQTRKLTDV ETQVLNQTSR LEIQLLENSL STYKLEKQLL QQTNEILKIH EKNSLLEHKI LEMEGKHKEE LDTLKEEKEN LQGLVTRQTY IIQELEKQLN RATTNNSVLQ KQQLELMDTV HNLVNLCTKE GVLLKGGKRE EEKPFRDCAD VYQAGFNKSG IYTIYINNMP EPKKVFCNMD VNGGGWTVIQ HREDGSLDFQ RGWKEYKMGF GNPSGEYWLG NEFIFAITSQ RQYMLRIELM DWEGNRAYSQ YDRFHIGNEK QNYRLYLKGH TGTAGKQSSL ILHGADFSTK DADNDNCMCK CALMLTGGWW FDACGPSNLN GMFYTAGQNH GKLNGIKWHY FKGPSYSLRS TTMMIRPLDF

      What applications can ANGPT1 Protein be used in?
      ANGPT1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for ANGPT1 Protein?
      The endotoxin level is minimal, ANGPT1 Protein was purified using conventional chromatography techniques.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Angpt1 Human
  • View Data Sheet

    Name :

    SERPING1 Human HEK

    Description:

    Serpin Peptidase Inhibitor, Clade G Member 1 Human Recombinant HEK

    C1IN, C1INH, C1NH, HAE1, HAE2 , Plasma protease C1 inhibitor, C1 esterase inhibitor, C1-inhibiting factor, Serpin G1, Name, SERPING1.

    Product # :

    PRO-1639

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    Description

    SERPING1 Human Recombinant produced by transfected human cells is a single polypeptide chain containing 486 amino acids (23-500). SERPING1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    SERPING1 was lyophilized from a 0.2 µM filtered solution of 20mM Tris-HCl and 150mM NaCl, pH 8.0.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Plasma protease C1 inhibitor (SERPING1) is a part of the serpin superfamily of serine protease inhibitors. SERPING1 plays an important role in regulating activation of both the complement and contact systems. That isdue to the fact that SERPING1 regulates the activation of complement factor C1 in addition to the activity of activated C1 by coupling with the active catalytic site at the light chains of C1r and C1s. SERPING1 insufficiency results in hereditary angioedema, which is characterized by recurrent episodes of localized angioedema of the skin, gastrointestinal mucosa or upper respiratory mucosa.

    • Synonyms

      C1IN, C1INH, C1NH, HAE1, HAE2 , Plasma protease C1 inhibitor, C1 esterase inhibitor, C1-inhibiting factor, Serpin G1, Name, SERPING1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SERPING1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SERPING1 should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized SERPING1 in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      NPNATSSSSQDPESLQDRGEGKVATTVISKMLFVEPILEVSSLPTTNSTTNSATKITANTTDEPTTQPTT
      EPTTQPTIQPTQPTTQLPTDSPTQPTTGSFCPGPVTLCSDLESHSTEAVLGDALVDFSLKLYHAFSAMKK
      VETNMAFSPFSIASLLTQVLLGAGENTKTNLESILSYPKDFTCVHQALKGFTTKGVTSVSQIFHSPDLAI
      RDTFVNASRTLYSSSPRVLSNNSDANLELINTWVAKNTNNKISRLLDSLPSDTRLVLLNAIYLSAKWKTT
      FDPKKTRMEPFHFKNSVIKVPMMNSKKYPVAHFIDQTLKAKVGQLQLSHNLSLVILVPQNLKHRLEDMEQ
      ALSPSVFKAIMEKLEMSKFQPTLLTLPRIKVTTSQDMLSIMEKLEFFDFSYDLNLCGLTEDPDLQVSAMQ
      HQTVLELTETGVEAAAASAISVARTLLVFEVQQPFLFMLWDQQHKFPVFMGRVYDPRAVDHHHHHH

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Serping1 Human Hek
  • View Data Sheet

    Name :

    ANXA10 Human

    Description:

    Annexin A10 Human Recombinant

    Annexin A10, Annexin-10, Annexin-14, ANXA10, ANX14.

    Product # :

    PRO-1045

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    Description

    ANXA10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 348 amino acids (1-324 a.a.) and having a molecular mass of 39.8kDa.ANXA10 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ANXA10 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 1mM DTT and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      Annexin A10 (ANXA10) is a member of the annexin family of calcium-binding proteins that contains a few members which are described by a conserved core domain that binds phospholipids in a Ca2+-dependent manner, and a unique amino-terminal region, which may convene binding specificity. The ANXA10 protein contains 4 annexin domains and might be required in the regulation of cellular growth and signal transduction pathways throughout the cell.

    • Synonyms

      Annexin A10, Annexin-10, Annexin-14, ANXA10, ANX14.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMFCGDY VQGTIFPAPN FNPIMDAQML GGALQGFDCD KDMLINILTQ RCNAQRMMIA EAYQSMYGRD LIGDMREQLS DHFKDVMAGL MYPPPLYDAH ELWHAMKGVG TDENCLIEIL ASRTNGEIFQ MREAYCLQYS NNLQEDIYSE TSGHFRDTLM
      NLVQGTREEG YTDPAMAAQD AMVLWEACQQ KTGEHKTMLQ MILCNKSYQQ LRLVFQEFQN ISGQDMVDAI NECYDGYFQE LLVAIVLCVR DKPAYFAYRL YSAIHDFGFH NKTVIRILIA RSEIDLLTIR KRYKERYGKS LFHDIRNFAS GHYKKALLAI CAGDAEDY.

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    Anxa10 Human
  • View Data Sheet

    Name :

    SHH Mouse, His

    Description:

    Sonic HedgeHog Mouse Recombinant, His Tag

    SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.

    Product # :

    CYT-711

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    Description

    SHH Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 183 amino acids (25-198 a.a.) and having a molecular mass of 20.8 kDa. SHH protein is fused to a 8 amino acid His-Tag at C-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    SHH Mouse His Tag solution containing 20mM Trsi HCL pH-8, 1mM DTT, and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Recombinant Human Sonic Hedgehog is part of a small group of secreted proteins that are vital for development in both vertebrates and invertebrates. 3 mammalian hedgehog genes (sonic, desert, Indian) share about 60% homology. The Human Sonic Hedgehog is 99% homologous to the mouse gene. Sonic HedgeHog is a protein that is vital in guding the early embryo. It has been associated as the major inductive signal in patterning of the ventral neural tube, the anterior-posterior limb axis, and the ventral somites. Sonic HedgeHog binds to the patched receptor, which functions in association with smoothened, to activate the transcription of target genes. In the absence of sonic HedgeHog, patched receptor represses the constitutive signaling activity of smoothened. Sonic HedgeHog also regulates another factor, the gli oncogene. Sonic HedgeHog intercellular signal is essential for a various patterning events during development: signal produced by the notochord that induces ventral cell fate in the neural tube and somites, and the polarizing signal for patterning of the anterior-posterior axis of the developing limb bud. Sonic HedgeHog exhibits both floor plate- and motor neuron-inducing activity. Mutations in a long-range Sonic HedgeHog enhancer located in an intron of the limb region 1 gene result in preaxial polydactyly.

    • Synonyms

      SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MCGPGRGFGK RRHPKKLTPL AYKQFIPNVA EKTLGASGRY EGKITRNSER FKELTPNYNP DIIFKDEENT GADRLMTQRC KDKLNALAIS VMNQWPGVKL RVTEGWDEDG HHSEESLHYE GRAVDITTSD RDRSKYGMLA RLAVEAGFDW VYYESKAHIH CSVKAENSVA AKSGGLEHHH HHH.

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    Shh Mouse His
  • View Data Sheet

    Name :

    BIRC5 Human

    Description:

    Baculoviral IAP Repeat-Containing 5 Human Recombinant

    BIRC-5, Baculoviral IAP repeat-containing protein 5, API4, EPR-1, Apoptosis inhibitor survivin, Apoptosis inhibitor 4, BIRC5, IAP4, Survivin.

    Product # :

    PRO-613

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    Description

    Survivin Human Recombinant fused to a 152 a.a. N-terminal CaM-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 294 amino acids (1-142 a.a.) and having a molecular mass of 33 kDa.

    Source

    Escherichia Coli.

    Formulation

    The BIRC5 solution contains 20mM Tris-HCl pH-7.5 & 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Survivin is part of the of the inhibitor of apoptosis (IAP) family, which encodes negative regulatory proteins that prevent apoptotic cell death. Members of the IAP family include multiple baculovirus IAP repeat (BIR) domains, but Survivin has only a single BIR domain.
      Survivin is an inhibitor of caspase activation therefore leading to negative regulation of apoptosis. BIRC5 is expressed in Merkel cell carcinoma.
      BIRC5 polymorphism causes survivin expression, thus contributing to the genetic susceptibility to lung cancer. BIRC5 expression in large cell lung cancer is substantially higher than in normal tissue cells. Survivin mRNA is up-regulated in tumors. Apoptotic response of infected intestinal epithelial cells is suppressed by C. parvum via upregulation of BIRC5, favoring parasite infection. Up-regulation of of Survivin is associated with breast carcinomas.
      BIRC5 increases the activity of an oncolytic adenovirus in the presence of low-dose radiotherapy. ER- breast cancer cells become dependent on Notch-survivin signaling for their maintenance, in vivo. Survivin mRNA positive cases are related with bladder tumour recurrence elevated expression of survivin might play an important role of development in nasal polyps.

    • Synonyms

      BIRC-5, Baculoviral IAP repeat-containing protein 5, API4, EPR-1, Apoptosis inhibitor survivin, Apoptosis inhibitor 4, BIRC5, IAP4, Survivin.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE EVDEMIREAD IDGDGQVNYE EFVQMMTAKG SHMGAPTLPP AWQPFLKDHR ISTFKNWPFL EGCACTPERM AEAGFIHCPT ENEPDLAQCF FCFKELEGWE PDDDPIEEHK KHSSGCAFLS VKKQFEELTL GEFLKLDRER AKNKIAKETN NKKKEFEETA KKVRRAIEQL AAMD.

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    Birc5 Human
  • View Data Sheet

    Name :

    Streptavidin (37-159), His

    Description:

    Streptavidin (37-159 a.a) Recombinant, His Tag

    Product # :

    PRO-1495

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    Description

    Streptavidin Recombinant produced in E. coli is a single polypeptide chain containing 148 amino acids (37-159) and having a molecular mass of 15.6kDa. Streptavidin is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The Streptavidin solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is widely used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMAEAGI TGTWYNQLGS TFIVTAGADG ALTGTYESAV GNAESRYVLT GRYDSAPATD GSGTALGWTV AWKNNYRNAH SATTWSGQYV GGAEARINTQ WLLTSGTTEA NAWKSTLVGH DTFTKVKP.

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    Streptavidin 37 159 His
  • View Data Sheet

    Name :

    FGB Human

    Description:

    Fibrinogen Beta Chain Human Recombinant

    Fibrinogen beta chain, Fibrinopeptide B, Fibrinogen, B Beta Polypeptide, Epididymis Secretory Sperm Binding Protein Li 78p, HEL-S-78p.

    Product # :

    PRO-2210

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    Description

    FGB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 351 amino acids (164-491a.a) and having a molecular mass of 40kDa. FGB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FGB protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Fibrinogen Beta Chain 9 (FGB) is the beta component of fibrinogen, a blood-borne glycoprotein composed of 3 pairs of nonidentical polypeptide chains. When vascular injury accrues, fibrinogen is cleaved by thrombin to form fibrin which is found in abundance in blood clots.

    • Synonyms

      Fibrinogen beta chain, Fibrinopeptide B, Fibrinogen, B Beta Polypeptide, Epididymis Secretory Sperm Binding Protein Li 78p, HEL-S-78p.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSDNENVVN EYSSELEKHQ LYIDETVNSN IPTNLRVLRS ILENLRSKIQ KLESDVSAQM EYCRTPCTVS CNIPVVSGKE CEEIIRKGGE TSEMYLIQPD SSVKPYRVYC DMNTENGGWT VIQNRQDGSV DFGRKWDPYK QGFGNVATNT DGKNYCGLPG EYWLGNDKIS QLTRMGPTEL LIEMEDWKGD KVKAHYGGFT VQNEANKYQI SVNKYRGTAG NALMDGASQL MGENRTMTIH NGMFFSTYDR DNDGWLTSDP RKQCSKEDGG GWWYNRCHAA NPNGRYYWGG QYTWDMAKHG TDDGVVWMNW KGSWYSMRKM SMKIRPFFPQ Q.

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    Fgb Human
  • View Data Sheet

    Name :

    FGF 8 Human

    Description:

    Fibroblast Growth Factor-8 Human Recombinant

    FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.

    Product # :

    CYT-839

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    Description

    FGF 8 Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 194 amino acids and having a total molecular mass of 22.5kDa.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a sterile 0.2 micron filtered aqueous solution containing 0.1% TFA.

    Purity

    Greater than 95.0% as determined by analysis by SDS-PAGE.

    Biological Activity

    The ED50, as determined by its ability to induce proliferation of NR6-R 3T3, is 0.915ng/ml, corresponding to a specific activity of 1.1x106units/mg.

    More Info

    • Introduction

      FGF8 is part of the fibroblast growth factor family. FGF family members have wide mitogenic and cell survival activities, and participate in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF8 supports androgen and anchorage independent growth of mammary tumor cells. FGF8 over expression increases tumor growth and angiogensis. The adult expression of FGF-8 gene is restricted to testes and ovaries. FGF8 functions as an embryonic epithelial factor. FGF8 takes part in midbrain and limb development, organogenesis, embryo gastrulation and left-right axis determination.

    • Synonyms

      FGF8B, FGF-8B, FGF8-B, KAL6, HBGF-8, HBGF8, AIGF, HBGF-8, MGC149376, fibroblast growth factor 8.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FGF-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-8 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized FGF-8 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MQVTVQSSPN FTQHVREQSL VTDQLSRRLI RTYQLYSRTS GKHVQVLANK RINAMAEDGDPFAKLIVETD TFGSRVRVRG AETGLYICMN KKGKLIAKSN GKGKDCVFTE IVLENNYTAL QNAKYEGWYM AFTRKGRPRK GSKTRQHQRE VHFMKRLPRG HHTTEQSLRF EFLNYPPFTR SLRGSQRTWA PEPR.

    • Background

      What is the molecular weight/Mw of FGF8 Protein?
      FGF8 Protein has a total Mw of 22.5kDa.

      What is the source or expression system of FGF8 Protein?
      Escherichia Coli.

      What is the Purity of FGF8 Protein?
      FGF8 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF8 Protein?
      The ED50, as determined by its ability to induce proliferation of NR6-R 3T3, is 0.915ng/ml, corresponding to a specific activity of 1.1x106units/mg.

      What is the amino acid sequence of FGF8 Protein?
      MQVTVQSSPN FTQHVREQSL VTDQLSRRLI RTYQLYSRTS GKHVQVLANK RINAMAEDGDPFAKLIVETD TFGSRVRVRG AETGLYICMN KKGKLIAKSN GKGKDCVFTE IVLENNYTAL QNAKYEGWYM AFTRKGRPRK GSKTRQHQRE VHFMKRLPRG HHTTEQSLRF EFLNYPPFTR SLRGSQRTWA PEPR.

      What applications can FGF8 Protein be used in?
      FGF8 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF8 Protein?
      The endotoxin level is minimal, FGF8 Protein was purified using conventional chromatography techniques.

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    Fgf 8 Human
  • View Data Sheet

    Name :

    CALB2 Human

    Description:

    Calbindin-2 Human Recombinant

    Calretinin, CR, CALB2, CAB29, CAL2, CaBP29K, 29 kDa calbindin.

    Product # :

    PRO-401

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    Description

    CALB2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 291 amino acids (1-271 a.a.) and having a molecular mass of 33.7kDa.The CALB2 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CALB2 1mg/ml protein solution contains 20mM Tris-HCl buffer pH-8 & 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Calretinin is an intracellular calcium-binding protein belonging to the troponin C superfamily characterized by a structural motif described as the EF-hand domain. The immunohistochemical detection of calretinin in developing cerebellum is restricted to the later stages indicated by weak staining from week 21 of gestation, in Purkinje and basket cells and in neurons of the dentate nucleus. The intensity of staining increases as the cerebellum matures. In tumors, calretinin has been detected in mesotheliomas and some pulmonary adenocarcinomas.

    • Synonyms

      Calretinin, CR, CALB2, CAB29, CAL2, CaBP29K, 29 kDa calbindin.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAGPQQQPPY LHLAELTASQ FLEIWKHFDA DGNGYIEGKE LENFFQELEK ARKGSGMMSK SDNFGEKMKE FMQKYDKNSD GKIEMAELAQ ILPTEENFLL CFRQHVGSST EFMEAWRKYD TDRSGYIEAN ELKGFLSDLL KKANRPYDEP KLQEYTQTIL RMFDLNGDGK LGLSEMSRLL PVQENFLLKF QGMKLTSEEF NAIFTFYDKD RSGYIDEHEL DALLKDLYEK NKKEMNIQQL TNYRKSVMSL AEAGKLYRKD LEIVLCSEPP M.

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    Calb2 Human
  • View Data Sheet

    Name :

    KLK7 Human

    Description:

    Kallikrein-7 Human Recombinant

    kallikrein-related peptidase 7, SCCE, hSCCE, EC 3.4.21.117, hK7, Kallikrein-7, PRSS6, KLK7.

    Product # :

    ENZ-510

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    Description

    KLK7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 249 amino acids (30-253) and having a molecular mass of 27.1 kDa.The KLK7 is fused to a 25 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    KLK7 protein 1mg/ml is supplied in 20mM Tris-HCl, pH-8, 2M Urea and 10% Glycerol.

    Purity

    Greater than 90.0% as determined by Analysis by SDS-PAGE.

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    • Introduction

      KLK7 catalyzes the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. Specific for amino acid residues with aromatic side chains in the P1 position. KLK7 is involved in the activation of precursors to inflammatory cytokines.

    • Synonyms

      kallikrein-related peptidase 7, SCCE, hSCCE, EC 3.4.21.117, hK7, Kallikrein-7, PRSS6, KLK7.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMIIDGA PCARGSHPWQ VALLSGNQLH CGGVLVNERW VLTAAHCKMN EYTVHLGSDT LGDRRAQRIK ASKSFRHPGY STQTHVNDLM LVKLNSQARL SSMVKKVRLP SRCEPPGTTC TVSGWGTTTS PDVTFPSDLM CVDVKLISPQ DCTKVYKDLL ENSMLCAGIP DSKKNACNGD SGGPLVCRGT LQGLVSWGTF PCGQPNDPGV YTQVCKFTKW INDTMKKHR.

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    Klk7 Human
  • View Data Sheet

    Name :

    CFL1 Human

    Description:

    Cofilin-1 Human Recombinant

    CFL-1, CFL1, Cofilin1, Cofilin-1, Cofilin, non-muscle isoform, 18 kDa phosphoprotein, p18.

    Product # :

    PRO-591

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    Description

    Cofilin1 Human Recombinant (aa 1-166) fused to a 20 aa N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing a total of 186 amino acids and having a molecular mass of 20kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 20mM Tris pH-8 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by Analysis by SDS-PAGE.

    More Info

    • Introduction

      Cofilin is a family of actin-binding proteins which disassembles actin filaments. It is a widely distributed intracellular actin-modulating protein that binds and depolymerizes filamentous F-actin and inhibits the polymerization of monomeric G-actin in a pH-dependent manner. It is involved in the translocation of actin-cofilin complex from cytoplasm to nucleus.

    • Synonyms

      CFL-1, CFL1, Cofilin1, Cofilin-1, Cofilin, non-muscle isoform, 18 kDa phosphoprotein, p18.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCLSEDKKNIILE EGKEILVGDV GQTVDDPYAT FVKMLPDKDC RYALYDATYE TKESKKEDLVFIFWAPESAP LKSKMIYASS KDAIKKKLTG IKHELQANCY EEVKDRCTLA EKLGGSAVIS LEGKPL.

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    Cfl1 Human
  • View Data Sheet

    Name :

    GNMT Human

    Description:

    Glycine N-methyltransferase Human Recombinant

    Glycine N-methyltransferase, GNMT.

    Product # :

    ENZ-386

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    Description

    GNMT Human Recombinant fused with 20 amino acid His-Tag tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing a total of 315 amino acids (1-295 a.a.) and having a molecular mass of 34.9 kDa.The GNMT is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GNMT solution contains 20mM Tris pH 8.0 & 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GNMT is an enzyme that catalyzes the conversion of S-adenosyl-L-methionine with glycine to S-adenosyl-L-homocysteine. GNMT is located in the cytoplasm and acts as a homotetramer. Defects in the GNMT gene causes of GNMT deficiency (hypermethioninemia). GNMT affects DNA methylation by regulating the ratio of S-adenosylmethionine to S-adenosylhomocystine and is involved in the detoxification pathway in liver cells. GNMT expression is diminished in human hepatocellular carcinoma (HCC). GNMT catalyzes the methylation of glycine by using s- adenosylmethionine (adomet) to form n-methylglycine with the concomitant production of s-adenosylhomocysteine (adohcy). GNMT plays an essential role in the regulation of tissue concentration of adomet and of metabolism of methionine.

    • Synonyms

      Glycine N-methyltransferase, GNMT.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MVDSVYRTRS LGVAAEGLPD QYADGEAARV WQLYIGDTRS RTAEYKAWLL GLLRQHGCQR VLDVACGTGV DSIMLVEEGF SVTSVDASDK MLKYALKERW NRRHEPAFDK WVIEEANWMT LDKDVPQSAE GGFDAVICLG NSFAHLPDCK GDQSEHRLAL KNIASMVRAG GLLVIDHRNY DHILSTGCAP PGKNIYYKSD LTKDVTTSVL IVNNKAHMVT LDYTVQVPGA GQDGSPGLSK FRLSYYPHCL ASFTELLQAA FGGKCQHSVL GDFKPYKPGQ TYIPCYFIHV LKRTD.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Gnmt Human
  • View Data Sheet

    Name :

    LXN Mouse

    Description:

    Latexin Mouse Recombinant

    Latexin, Endogenous carboxypeptidase inhibitor, ECI, Tissue carboxypeptidase inhibitor, TCI.

    Product # :

    PRO-2218

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    Description

    LXN Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 245 amino acids (1-222 a.a) and having a molecular mass of 27.9kDa. LXN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LXN protein solution (1mg/ml) containing Phosphate Buffer Saline (pH7.4), 30% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lxn also known as Latexin is a member of the protease inhibitor I47 (latexin) family. Lxn's function is hardly reversible, non-competitive, as well as potent inhibitor of CPA1, CPA2 and CPA4. Furthermore, Lxn plays a role in inflammation. Among the diseases associated with LXN are endocervicitis and listeriosis.

    • Synonyms

      Latexin, Endogenous carboxypeptidase inhibitor, ECI, Tissue carboxypeptidase inhibitor, TCI.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMEIPPTH YAASRAASVA ENCINYQQGT PHKLFLVQTV QQASKEDIPG RGHKYHLKFS VEEIIQKQVT VNCTAEVLYP QMGQGSAPEV NFTFEGEIGK NPDEEDNTFY QSLMSLKRPL EAQDIPDNFG NVSPQMKPVQ HLAWVACGYV MWQNSTEDTW YKMLKIQTVK QVQRNDDFIE LDYTILLHDI ASQEIIPWQM QVLWHPQYGT KVKHNSRLPK EGQAE.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Lxn Mouse
  • View Data Sheet

    Name :

    VAMP2 Human

    Description:

    Synaptobrevin-2 Human Recombinant

    Vesicle-associated membrane protein 2, SYB2, VAMP-2, Synaptobrevin-2, VAMP2, FLJ11460.

    Product # :

    PRO-578

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    Description

    VAMP2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 126 amino acids (1-89) and having a molecular mass of 13.8 kDa. The VAMP contains 37 amino acids His-Tag fused at N-terminus and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution (1mg/ml) contains 1X PBS pH 7.4 and 1mM EDTA.

    Purity

    Greater than 95.0% as dtermined by SDS-PAGE.

    More Info

    • Introduction

      Synaptobrevin 2 which is an 18 kDa integral membrane protein localized to the cytoplasmic surface of synaptic vesicle, consists of a proline-rich N-terminal region, a highly conserved hydrophilic domain, followed by a transmembrane anchor and a C-terminal. Synaptobrevin 2 is predominantly expressed in Langerhans islets and glomerular cells. The N-terminal domain of the protein (residues 1-89) forms a specific SNARE complex with the target membrane-associated t- or Q-SNAREs syntaxin 1 and SNAP-25.

    • Synonyms

      Vesicle-associated membrane protein 2, SYB2, VAMP-2, Synaptobrevin-2, VAMP2, FLJ11460.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMSA TAATAPPAAP AGEGGPPAPP PNLTSNRRLQ QTQAQVDEVV DIMRVNVDKV LERDQKLSEL DDRADALQAG ASQFETSAAK LKRKYW.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Vamp2 Human
  • View Data Sheet

    Name :

    VAMP3 Human

    Description:

    Synaptobrevin-3 Human Recombinant

    VAMP3, VAMP-3, Cellubrevin, Vesicle-Associated Membrane Protein 3, Synaptobrevin-3, CEB, SYB3.

    Product # :

    PRO-652

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    Description

    VAMP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids and having a molecular mass of 8.7 kDa.

    Source

    Escherichia Coli.

    Formulation

    The VAMP3 protein solution contains 20mM Tris pH-7.5 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      VAMP3 is present in recycling endosomes and endosome-derived vesicles. VAMP3 has been implicated in recycling of transferrin receptors to the plasma membrane, secretion of alpha-granules in platelets, recycling of T-cell receptors to the immunological synapses, and membrane trafficking during cell migration. VAMP-3 is present in human platelets and necessary for granule secretion. Synaptobrevins are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. VAMP3 high homology to other VAMPs in its broad tissue distribution and subcellular localization is shown to be the human equivalent of the rodent cellubrevin. In platelets the protein resides on a compartment that is not mobilized to the plasma membrane on calcium or thrombin stimulation.

    • Synonyms

      VAMP3, VAMP-3, Cellubrevin, Vesicle-Associated Membrane Protein 3, Synaptobrevin-3, CEB, SYB3.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MSTGPTAATG SNRRLQQTQN QVDEVVDIMR VNVDKVLERD QKLSELDDRA DALQAGASQF ETSAAKLKRK YWWKNCK.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Vamp3 Human
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