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  • Cytokines
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  • Tumor Necrosis Factor

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    B type Natriuretic Peptide

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    Betacellulin

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  • MEC (CCL28)

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    CTACK (CCL27)

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    ENA-78 (CXCL5)

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    Eotaxin (CCL11,24,26)

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Search results

192 results found for “Neuronal Calcium Sensor”

Name

Description

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  • View Data Sheet

    Name :

    S100A4 Human

    Description:

    S100 Calcium-Binding Protein A4 Human Recombinant

    Protein S100-A4, S100 calcium-binding protein A4, Metastasin, Protein Mts1, Placental calcium-binding protein, Calvasculin, S100A4, CAPL, MTS1, 42A, 18A2, FSP1, P9KA, PEL98.

    Product # :

    PRO-698

    Price :

    Quantity :

    Shipping Method :

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    Description

    S100A4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 121 amino acids (1-101) and having a molecular mass of 13.8 kDa.The S100A4 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    S100A4 protein at in 20mM Tris-HCl, pH-8 & 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      S100A4 is part of the S100 super-family of proteins containing 2 EF-hand calcium binding domains. S100A4 is ubiquitously overexpressed and is localized in the cytoplasm and/or nucleus. S100A4 is involved in motility, invasion, and tubulin polymerization. Chromosomal rearrangements and altered expression of the S100A4 gene have been implicated in tumor metastasis.

    • Synonyms

      Protein S100-A4, S100 calcium-binding protein A4, Metastasin, Protein Mts1, Placental calcium-binding protein, Calvasculin, S100A4, CAPL, MTS1, 42A, 18A2, FSP1, P9KA, PEL98.

    • 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 MACPLEKALD VMVSTFHKYS GKEGDKFKLN KSELKELLTR ELPSFLGKRT DEAAFQKLMS NLDSNRDNEVDFQEYCVFLS CIAMMCNEFF EGFPDKQPRK K.

    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.

    S100A4 Human His
  • View Data Sheet

    Name :

    NT 3 Human

    Description:

    Neurotrophin-3 Human Recombinant

    Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3.

    Product # :

    CYT-257

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • More Info

    Description

    Neurotrophin-3 Human Recombinant produced in E.Coli is a non-glycosylated and non-covalently linked homodimer, containing 2x120 amino acid chains, having a total Mw of 27.5 kDa. The NT-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from 0.1% TFA.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependent proliferation of neuroblastoma cell line expressing BR6 is 3.49 ng/ml.

    More Info

    • Introduction

      NT3 a member of the neurotrophin family, that controls survival and differentiation of mammalian neurons. This protein is closely related to both nerve growth factor and brain-derived neurotrophic factor. It may be involved in the maintenance of the adult nervous system, and may affect development of neurons in the embryo when it is expressed in human placenta. NTF3-deficient mice generated by gene targeting display severe movement defects of the limbs. The mature peptide of this protein is identical in all mammals examined including human, pig, rat and mouse.

    • Synonyms

      Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized NGF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NGF-2 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 Neurotrophin-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MYAEHKSHRGE YSVCDSESLW VTDKSSAIDI RGHQVTVLGE IKTGNSPVKQ YFYETRCKEA RPVKNGCRGI DDKHWNSQCK TSQTYVRALT SENNKLVGWR WIRIDTSCVC ALSRKIGRT.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 2.165 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of NT-3 as a Reference Standard.

    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.

    Neurotrophin 3 Human
  • View Data Sheet

    Name :

    PSPN Mouse

    Description:

    Persephin Mouse Recombinant

    Persephin, PSPN.

    Product # :

    CYT-802

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
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    • purity
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    • More Info

    Description

    PSPN Mouse Recombinant produced in E.Coli is a disulfide-linked homodimer containing 2x96 amino acids and having a molecular mass of 20.7kDa. The PSPN is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2?m filtered concentrated solution in 30 %ACN, 0.1 %TFA, 150mM NaCl.

    Purity

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

    Biological Activity

    Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using human TT medullary thyroid cancer cells is less than 0.1ng/ml, corresponding to a specific activity of > 1.0 × 10,000,000 IU/mg. 

    More Info

    • Introduction

      Persephin is a member of the GDNF ligand subfamily of the TGF-beta superfamily. PSPN encourages the existence and growth of key dopaminergic and motor neurons, as well as taking part in kidney development. Nonetheless, persephin does not support existence of peripheral neurons.

    • Synonyms

      Persephin, PSPN.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized PSPN although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PSPN 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 PSPN in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ALAGSCRLWS LTLPVAELGL GYASEEKVIF RYCAGSCPQE ARTQHSLVLA RLRGRGRAHG RPCCQPTSYA DVTFLDDQHH WQQLPQLSAA ACGCGG

    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.

    Pspn Mouse
  • View Data Sheet

    Name :

    BASP1 Human

    Description:

    Brain Abundant Membrane Attached Signal Protein 1 Human Recombinant

    CAP-23, CAP23, NAP-22, NAP22, Brain acid soluble protein 1, BASP1, BASP1 Human, 22 kDa neuronal tissue-enriched acidic protein, Neuronal axonal membrane protein NAP-22.

    Product # :

    PRO-1355

    Price :

    Quantity :

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    • description
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    Description

    BASP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 250 amino acids (1-227) and having a molecular mass of 25 kDa (Molecular size on SDS-PAGE will appear higher). BASP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BASP1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Brain Abundant Membrane Attached Signal Protein 1 (BASP1) is a membrane bound protein with numerous transient phosphorylation positions and PEST motifs. Preservation of proteins with PEST sequences amongst diverse species supports their functional significance. PEST sequences take place in proteins with high turnover rates. Immunological attributes of this protein are species specific. BASP1 undergoes N-terminal myristoylation.

    • Synonyms

      CAP-23, CAP23, NAP-22, NAP22, Brain acid soluble protein 1, BASP1, BASP1 Human, 22 kDa neuronal tissue-enriched acidic protein, Neuronal axonal membrane protein NAP-22.

    • 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 MGSMGGKLSK KKKGYNVNDE KAKEKDKKAE GAATEEEGTP KESEPQAAAE PAEAKEGKEK PDQDAEGKAE EKEGEKDAAA AKEEAPKAEP EKTEGAAEAK AEPPKAPEQE QAAPGPAAGG EAPKAAEAAA APAESAAPAA GEEPSKEEGE PKKTEAPAAP AAQETKSDGA PASDSKPGSS EAAPSSKETP AATEAPSSTP KAQGPAASAE EPKPVEAPAA NSDQTVTVKE.

    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.

    Basp1 Human
  • View Data Sheet

    Name :

    NEURL2 Human

    Description:

    Neuralized Homolog 2 Human Recombinant

    800x600 800x600 800x600 neuralized homolog 2, C20orf163, OZZ, Ozz-E3, Neuralized-like protein 2, Neuralized Homolog 2, NEURL2. Normal 0 false false false EN-US X-NONE HE MicrosoftInternetExplorer4 /* Style Definitions */ table.MsoNormalTable {mso-style-name:"Table Normal"; mso-tstyle-rowband-size:0; mso-tstyle-colband-size:0; mso-style-noshow:yes; mso-style-priority:99; mso-style-parent:""; mso-padding-alt:0cm 5.4pt 0cm 5.4pt; mso-para-margin:0cm; mso-para-margin-bottom:.0001pt; mso-pagination:widow-orphan; font-size:10.0pt; font-family:"Calibri","sans-serif";}

    Product # :

    PRO-1678

    Price :

    Quantity :

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    • description
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    Description

    NEURL2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 308 amino acids (1-285) and having a molecular mass of 34.1 kDa.NEURL2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NEURL2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Neuralized Homolog 2 (NEURL2) takes part in the process of myofiber differentiation and maturation. NEURL2 is probable substrate-recognition component of a SCF-like ECS E3 ubiquitin-protein ligase complex, which mediates the ubiquitination of proteins. NEURL2 contributes to catalysis through recognition and positioning of the substrate and the ubiquitin-conjugating enzyme. NEURL2 regulates the ubiquitin-mediated degradation of beta-catenin during myogenesis.

    • Synonyms

      neuralized homolog 2, C20orf163, OZZ, Ozz-E3, Neuralized-like protein 2, Neuralized Homolog 2, NEURL2.

    • 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 MGSMAAASEP VDSGALWGLE RPEPPPTRFH RVHGANIRVD PSGTRATRVE SFAHGVCFSR EPLAPGQVFL VEIEEKELGW CGHLRLGLTA LDPASLAPVP EFSLPDLVNL GHTWVFAITR HHNRVPREGR PEAEAAAPSR PPTLLVEPYL RIEQFRIPRD
      RLVGRSRPGL YSHLLDQLYE LNVLPPTARR SRLGVLFCPR PDGTADMHII INGEDMGPSA RGLPAAQPLY AVVDVFASTK SVRLVQLEYG LPSLQTLCRL VIQRSMVHRL AIDGLHLPKE LKDFCKYE.

    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.

    Neurl2 Human
  • View Data Sheet

    Name :

    CALB2 Antibody

    Description:

    Calbindin-2, Mouse Anti Human

    Calretinin, CR, Calb2, calbindin 2.

    Product # :

    ANT-667

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    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

    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, calbindin 2.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human CALB2 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human CALB2 protein 1-271 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      PAT5C5AT.

    • Applications

      The antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      CALB2 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

    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.

    Calb2 Antibody
  • View Data Sheet

    Name :

    NEDD8 Human

    Description:

    Neural Precursor Cell Expressed Developmentally Down-Regulated 8 Human Recombinant

    Nedd-8, FLJ43224, MGC104393, MGC125896, MGC125897, NEDD8, Ubiquitin-like protein Nedd8, Neddylin, Neural precursor cell expressed developmentally down-regulated protein 8.

    Product # :

    ENZ-396

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    Description

    NEDD8 Human Recombinant fused with 37 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 113 amino acids (1-76 a.a.) and having a molecular mass of 12.8 kDa.The NEDD8 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NEDD8 solution contains 20mM Tris pH 8.0, 50mM NaCl, 0.5mM DTT & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NEDD8 is part of the ubiquitin family. Human NEDD8 shares 60% amino acid sequence homology to ubiquitin. The NEDD8 system is essential for the regulation of protein degradation pathways involved in cell cycle progression, morphogenesis and tumorigenesis. NEDD8 is involved in cell cycle control and embryogenesis. Covalent attachment to its substrates requires prior activation by the E-1 complex UbE1c- appbp1 and linkage to the E-2 enzyme UbE2m. Attachment of NEDD8 to cullins activates their associated E-3 ubiquitin ligase activity, and thus promotes polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins.

    • Synonyms

      Nedd-8, FLJ43224, MGC104393, MGC125896, MGC125897, NEDD8, Ubiquitin-like protein Nedd8, Neddylin, Neural precursor cell expressed developmentally down-regulated protein 8.

    • 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

      MHHHHHHMKI EEGKLVIWIN GDKGYNGLAE VGKKFEKDTG IKVTVEHPDK LEEKFPQVAA TGDGPDIIFW AHDRFGGYAQ SGLLAEITPD KAFQDKLYPF TWDAVRYNGK LIAYPIAVEA LSLIYNKDLL PNPPKTWEEI PALDKELKAK GKSALMFNLQ EPYFTWPLIA ADGGYAFKYE NGKYDIKDVG VDNAGAKAGL TFLVDLIKNK HMNADTDYSI AEAAFNKGET AMTINGPWAW SNIDTSKVNY GVTVLPTFKG QPSKPFVGVL SAGINAASPN KELAKEFLEN YLLTDEGLEA
      VNKDKPLGAV ALKSYEEELA KDPRIAATME NAQKGEIMPN IPQMSAFWYA VRTAVINAAS GRQTVDEALK DAQTNSSSNN NNNNNNNNLG IEGRGSHMAA AEAANCIMEV SCGQAESSEK PNAEDMTSKD YYFDSYAHFG IHEEMLKDEV RTLTYRNSMF HNRHLFKDKV VLDVGSGTGILCMFAAKAGA RKVIGIECSS ISDYAVKIVK ANKLDHVVTI IKGKVEEVEL PVEKVDIIIS EWMGYCLFYE SMLNTVLHAR DKWLAPDGLI FPDRATLYVT AIEDRQYKDY KIHWWENVYG
      FDMSCIKDVA IKEPLVDVVD PKQLVTNACL IKEVDIYTVK VEDLTFTSPF CLQVKRNDYVHALVAYFNIE FTRCHKRTGF STSPESPYTH WKQTVFYMED YLTVKTGEEI FGTIGMRPNA KNNRDLDFTI DLDFKGQLCE LSCSTDYRMR.

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    Nedd8 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 :

    S100A5 Mouse

    Description:

    S100 Calcium Binding Protein A5 Mouse Recombinant

    Protein S100-A5, Protein S-100D, S100 calcium-binding protein A5, S100a5, S100d, S100D9.

    Product # :

    PRO-1084

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    Description

    S100A5 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 117 amino acids (1-93) and having a molecular mass of 13.4kDa.The S100A5 is fused to a 24 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    S100A5 protein (1mg/ml) is supplied in 20mM Tris-HCl buffer, pH8.0, 40% glycerol, 3mM DTT and 200mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      S100 calcium binding protein A5 (S100A5) belongs to the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 family members are localized in the cytoplasm and/or nucleus of a wide range of cells, and are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100A5 has a Ca2+ affinity 20-100 fold higher than the other S100 proteins investigated under identical conditions. Furthermore, S100A5 protein binds Zn2+ and Cu2+, and Cu2+ strongly which harms the binding of Ca2+. S100A5 is expressed in very limited regions of the adult brain.

    • Synonyms

      Protein S100-A5, Protein S-100D, S100 calcium-binding protein A5, S100a5, S100d, S100D9.

    • Physical Appearance

      S100A9 is supplied as a 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 MGSHMETPLE KALTTMVTTF HKYSGREGSK LTLSRKELKE LIKTELSLAE KMKESSIDNL MKSLDKNSDQ EIDFKEYSVF LTTLCMAYND FFLEDNK.

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    S100A5 Mouse
  • View Data Sheet

    Name :

    CA1 Human, Active

    Description:

    Carbonic Anhydrase-1 Human Recombinant, BioActive

    CA1, CA-I, CAB.

    Product # :

    ENZ-1137

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    Description

    CA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 281 amino acids (1-261) and having a molecular mass of 31.0 kDa. CA1 Humanis fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CA1 Human protein (1mg/ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) containing 1mM DTT, 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 300pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1.0pmole of 4-nitrophenyl acetate to 4-nitrophenol per minute at pH 8.0 at 37C.

    More Info

    • Introduction

      CA, also known as carbonic anhydrase is an enzyme. Its main function revolves around the CO2 + H2O HCO3- + H+ (conversion of carbon dioxide to bicarbonate & protons). CA has a zinc ion in its active site. The main function of CA is to keep acid-base balance in the blood stream and various tissues. This enzyme also assists Carbonic Anhydrase I to move CO2 to and from tissues.

    • Synonyms

      CA1, CA-I, CAB.

    • 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 MASPDWGYDD KNGPEQWSKL YPIANGNNQS PVDIKTSETK HDTSLKPISV SYNPATAKEI INVGHSFHVN FEDNDNRSVL KGGPFSDSYR LFQFHFHWGS TNEHGSEHTV DGVKYSAELH VAHWNSAKYS SLAEAASKAD GLAVIGVLMK VGEANPKLQK VLDALQAIKT KGKRAPFTNF DPSTLLPSSL DFWTYPGSLT HPPLYESVTW IICKESISVS SEQLAQFRSL LSNVEGDNAV PMQHNNRPTQ PLKGRTVRAS F.

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    Ca1 Enzyme
  • View Data Sheet

    Name :

    SERPINE2 Mouse

    Description:

    Plasminogen Activator Inhibitor-2 Mouse Recombinant

    Serpnie2, B230326M24Rik, PAI-1, PI-7, PI7, PN-1, Spi4, Glia-derived nexin, GDN,Peptidase inhibitor 7, Protease nexin 1, Protease nexin I, Serine protease-inhibitor 4, Serpin E2.

    Product # :

    ENZ-972

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    Description

    SERPINE2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 386 amino acids (20-397a.a.) and having a molecular mass of 42.9kDa. SERPINE2 is expressed with a 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    SERPINE2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      Plasminogen Activator Inhibitor-2 (Serpine2) which inhibits thrombin, plasmin and plasminogen activators is a part of the Serpin superfamily of the serine protease inhibitors. Serpine2 is able to transform human embryonic kidney cells into neuron-like cells. Furthermore, Serpine2's over expression in mice leads to progressive neuronal and motor dysfunction.

    • Synonyms

      Serpnie2, B230326M24Rik, PAI-1, PI-7, PI7, PN-1, Spi4, Glia-derived nexin, GDN,Peptidase inhibitor 7, Protease nexin 1, Protease nexin I, Serine protease-inhibitor 4, Serpin E2.

    • 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

      SQFNSLSLEE LGSNTGIQVF NQIIKSRPHE NVVVSPHGIA SILGMLQLGA DGKTKKQLST VMRYNVNGVG KVLKKINKAI VSKKNKDIVT VANAVFLRNG FKMEVPFAVR NKDVFQCEVQ NVNFQDPASA SESINFWVKN ETRGMIDNLL SPNLIDGALT RLVLVNAVYF KGLWKSRFQP ESTKKRTFVA GDGKSYQVPM LAQLSVFRSG STRTPNGLWY NFIELPYHGE SISMLIALPT ESSTPLSAII PHITTKTIDS WMNTMVPKRM QLVLPKFTAV AQTDLKEPLK ALGITEMFEP SKANFTKITR SESLHVSHIL QKAKIEVSED GTKASAATTA ILIARSSPPW FIVDRPFLFS IRHNPTGAIL FLGQVNKPLE HHHHHH.

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    Serpine2 Mouse
  • View Data Sheet

    Name :

    SPINK1 Human

    Description:

    Serine Peptidase Inhibitor Kazal Type 1 Human Recombinant

    Serine Peptidase Inhibitor Kazal Type 1, Pancreatic Secretory Trypsin Inhibitor, Tumor-Associated Trypsin Inhibitor, PCTT, TATI, Spink3, Serine Protease Inhibitor Kazal Type 1, TCP, PSTI.

    Product # :

    ENZ-724

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    Description

    SPINK1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 79 amino acids (24-79) and having a molecular mass of 8.6kDa.SPINK1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SPINK1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Trypsin inhibitor SPINK1 is secreted from pancreatic acinar cells into pancreatic fluid. SPINK1 has a role in inhibition of trypsin-catalyzed premature initiation of zymogens in the pancreas and the pancreatic duct. Alterations in SPINK1 gene are the cause for tropical calcific and pancreatitis hereditary pancreatitis.

    • Synonyms

      Serine Peptidase Inhibitor Kazal Type 1, Pancreatic Secretory Trypsin Inhibitor, Tumor-Associated Trypsin Inhibitor, PCTT, TATI, Spink3, Serine Protease Inhibitor Kazal Type 1, TCP, PSTI.

    • 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 MGSDSLGREA KCYNELNGCT KIYDPVCGTD GNTYPNECVL CFENRKRQTS ILIQKSGPC.

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    Spink1 Human
  • View Data Sheet

    Name :

    CHRNA3 Human

    Description:

    Cholinergic Receptor Nicotinic Alpha 3 Human Recombinant

    Cholinergic Receptor, Nicotinic, Alpha 3 (Neuronal), Cholinergic Receptor, Nicotinic, Alpha Polypeptide 3, NACHRA3, LNCR2, PAOD2, Neuronal Nicotinic Acetylcholine Receptor, Alpha3 Subunit, Neuronal Acetylcholine Receptor Subunit Alpha-3, Acetylcholine Receptor, Alpha 3 (Neuronal), Nicotinic, Neuronal acetylcholine receptor subunit alpha-3.

    Product # :

    PRO-2216

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    Description

    CHRNA3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (32-240 a.a) and having a molecular mass of 27kDa. CHRNA3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CHRNA3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cholinergic Receptor Nicotinic Alpha 3, also known as CHRNA3 is part of the nicotinic acetylcholine receptor family. Proteins of this family form pentameric complexes comprised of both alpha & beta subunits. Furthermore, CHRNA3 is ligand-gated ions channel which prticipates in neurotransmission. CHRNA3 has been associated with an increased risk of smoking initiation as well as an increased susceptibility to lung cancer.

    • Synonyms

      Cholinergic Receptor, Nicotinic, Alpha 3 (Neuronal), Cholinergic Receptor, Nicotinic, Alpha Polypeptide 3, NACHRA3, LNCR2, PAOD2, Neuronal Nicotinic Acetylcholine Receptor, Alpha3 Subunit, Neuronal Acetylcholine Receptor Subunit Alpha-3, Acetylcholine Receptor, Alpha 3 (Neuronal), Nicotinic, Neuronal acetylcholine receptor subunit alpha-3.

    • 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 MGSSEAEHRL FERLFEDYNE IIRPVANVSD PVIIHFEVSM SQLVKVDEVN QIMETNLWLK QIWNDYKLKW NPSDYGGAEF MRVPAQKIWK PDIVLYNNAV GDFQVDDKTK ALLKYTGEVT WIPPAIFKSS CKIDVTYFPF DYQNCTMKFG SWSYDKAKID LVLIGSSMNL KDYWESGEWA IIKAPGYKHD IKYNCCEEIY PDITYSLYIR RL.

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    Chrna3 Human
  • View Data Sheet

    Name :

    CHRNA6 Human

    Description:

    Cholinergic Receptor Nicotinic, Alpha 6 Human Recombinant

    CHNRA6, Neuronal acetylcholine receptor subunit alpha-6, CHRNA6.

    Product # :

    PRO-1878

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    Description

    CHRNA6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 250 amino acids (26-239 a.a) and having a molecular mass of 29.3kDa. CHRNA6 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CHRNA6 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cholinergic Receptor Nicotinic, Alpha 6 (CHRNA6) is a part of the nicotinic acetylcholine receptors (nAChRs) family. nAChRs are heteropentameric ligand-gated ion channels generating from the assembly of alpha and beta protein subunits. After binding acetylcholine, the AChRs respond by a major change in conformation which affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. CHRNA6 receptors have a rather selective localization to the nigrostriatal pathway.

    • Synonyms

      CHNRA6, Neuronal acetylcholine receptor subunit alpha-6, CHRNA6.

    • 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 KDRWGSKGCV GCATEERLFH KLFSHYNQFI RPVENVSDPV TVHFEVAITQ LANVDEVNQI METNLWLRHI WNDYKLRWDP MEYDGIETLR VPADKIWKPD IVLYNNAVGD FQVEGKTKAL LKYNGMITWT PPAIFKSSCP MDITFFPFDH QNCSLKFGSW TYDKAEIDLL IIGSKVDMND FWENSEWEII DASGYKHDIK YNCCEEIYTD ITYSFYIRRL.

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    Chrna6 Human
  • View Data Sheet

    Name :

    SPINK7 Human

    Description:

    Serine Peptidase Inhibitor Kazal Type 7 Human Recombinant

    Serine peptidase inhibitor Kazal type 7, ECG2, ECRG2, Serine protease inhibitor Kazal-type 7, Esophagus cancer-related gene 2 protein, ECRG-2, SPINK7.

    Product # :

    PRO-1507

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    Description

    SPINK7 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 89 amino acids (20-85) and having a molecular mass of 9.6 kDa.SPINK7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SPINK7 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol and 2mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Serine peptidase inhibitor Kazal type 7 (SPINK7) which includes one Kazal-like domain is most likely serine protease inhibitor. Diseases linked with SPINK7 include esophageal cancer, and oral squamous cell carcinoma

    • Synonyms

      Serine peptidase inhibitor Kazal type 7, ECG2, ECRG2, Serine protease inhibitor Kazal-type 7, Esophagus cancer-related gene 2 protein, ECRG-2, SPINK7.

    • 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 MGSSEAASLS PKKVDCSIYK KYPVVAIPCP ITYLPVCGSD YITYGNECHL CTESLKSNGR VQFLHDGSC.

    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.

    Spink7 Human
  • View Data Sheet

    Name :

    CAPNS1 Human

    Description:

    Calpain, Small Subunit 1 Human Recombinant

    Calpain Small Subunit 1, CAPN4, Calcium-Activated Neutral Proteinase Small Subunit, Calcium-Dependent Protease Small Subunit 1, Calpain Regulatory Subunit, CANP Small Subunit, CDPS, CSS1, Calcium-Dependent Protease Small Subunit, Calcium-Dependent Protease Small Subunit, Calpain 4 Small Subunit (30K), Calpain Small Polypeptide, Calpain Small Subunit 1, CALPAIN4, CANPS, CAPNS, CANP, CAPNS1.

    Product # :

    PRO-1965

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    Description

    CAPNS1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 208 amino acids (84-268) and having a molecular mass of 23.8 kDa.CAPNS1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CAPNS1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Calpain, Small Subunit 1 (CAPNS1) belongs to the calpain small subunit family. Calpains are a ubiquitous, well-conserved family of calcium-dependent, cysteine proteases, widely distributed in mammalian cells. Calpain families are implicated in neurodegenerative processes, considering that their activation can be triggered by calcium influx and oxidative stress. Calpains function as heterodimers, comprising a specific large catalytic subunit (calpain 1 subunit in Calpain I, and calpain 2 subunit in Calpain II), and a common small regulatory subunit encoded by the CAPNS1 gene. The CAPNS1 protein is vital for the stability and function of both calpain heterodimers, whose proteolytic activities influence numerous cellular functions including apoptosis, proliferation, migration, adhesion, and autophagy.

    • Synonyms

      Calpain Small Subunit 1, CAPN4, Calcium-Activated Neutral Proteinase Small Subunit, Calcium-Dependent Protease Small Subunit 1, Calpain Regulatory Subunit, CANP Small Subunit, CDPS, CSS1, Calcium-Dependent Protease Small Subunit, Calcium-Dependent Protease Small Subunit, Calpain 4 Small Subunit (30K), Calpain Small Polypeptide, Calpain Small Subunit 1, CALPAIN4, CANPS, CAPNS, CANP, CAPNS1.

    • 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 MGSRTHYSNI EANESEEVRQ FRRLFAQLAG DDMEVSATEL MNILNKVVTR HPDLKTDGFG IDTCRSMVAV MDSDTTGKLG FEEFKYLWNN IKRWQAIYKQ FDTDRSGTIC SSELPGAFEA AGFHLNEHLY NMIIRRYSDE SGNMDFDNFI SCLVRLDAMF RAFKSLDKDG TGQIQVNIQE WLQLTMYS.

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    Capns1 Human
  • View Data Sheet

    Name :

    CA10 Human

    Description:

    Carbonic Anhydrase X Human Recombinant

    Carbonic anhydrase-related protein 10, Carbonic anhydrase-related protein X, CA-RP X, CARP X, carbonic anhydrase X, Cerebral protein 15, hucep-15, epididymis secretory sperm binding protein, UNQ533/PRO1076.

    Product # :

    ENZ-1189

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    Description

    CA10 Human Recombinant is a single, glycosylated polypeptide chain containing 317 amino acids (22-328a.a) and having a molecular mass of 36.3kDa (calculated). CA10 is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    CA10 protein solution (0.5mg/ml) is filtered in Phosphate-Buffered Saline pH 7.4 and 10% (w/v) glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 150 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1pmole of pnitrophenyl acetate to p-nitrophenol per minute at pH8.0 at 37℃.

    More Info

    • Synonyms

      Carbonic anhydrase-related protein 10, Carbonic anhydrase-related protein X, CA-RP X, CARP X, carbonic anhydrase X, Cerebral protein 15, hucep-15, epididymis secretory sperm binding protein, UNQ533/PRO1076.

    • 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. Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      DGSMQQNSPK IHEGWWAYKE VVQGSFVPVP SFWGLVNSAW NLCSVGKRQS PVNIETSHMI FDPFLTPLRI NTGGRKVSGT MYNTGRHVSL RLDKEHLVNI SGGPMTYSHR LEEIRLHFGS EDSQGSEHLL NGQAFSGEVQ LIHYNHELYT NVTEAAKSPN GLVVVSIFIK VSDSSNPFLN RMLNRDTITR ITYKNDAYLL QGLNIEELYP ETSSFITYDG SMTIPPCYET ASWIIMNKPV YITRMQMHSL RLLSQNQPSQ IFLSMSDNFR PVQPLNNRCI RTNINFSLQG KDCPNNRAQK LQYRVNEWLL KHHHHHH

    • Background

      Carbonic anhydrases (CAs) are a family of enzymes that play a crucial role in regulating pH balance and carbon dioxide transport in various tissues and organs. Carbonic anhydrase X (CA10) is a less-studied member of this family, and this research aims to explore its structure, function, and implications in metabolism and disease. Understanding the molecular mechanisms and regulatory roles of CA10 can provide valuable insights into its potential as a therapeutic target for various disorders.

      Structure and Expression of Carbonic Anhydrase X:

      CA10, also known as mitochondrial carbonic anhydrase, is a membrane-associated protein predominantly found in the mitochondria of various tissues, including the liver, kidney, and brain. It possesses the characteristic zinc-binding catalytic domain found in other CAs. However, CA10 has distinct features, including a unique N-terminal mitochondrial targeting sequence, suggesting its specific role within mitochondria.

      Role of Carbonic Anhydrase X in Metabolism:

      CA10 is involved in the regulation of pH and bicarbonate concentrations within the mitochondrial matrix, impacting mitochondrial metabolism. It catalyzes the reversible hydration of carbon dioxide to bicarbonate, facilitating the exchange of carbon dioxide between the mitochondria and the cytoplasm. This process is vital for maintaining acid-base homeostasis and efficient energy production through oxidative phosphorylation.

      Implications of Carbonic Anhydrase X in Disease:

      Emerging evidence suggests that CA10 may be implicated in various pathological conditions. Alterations in CA10 expression or activity have been associated with metabolic disorders, including obesity and diabetes. Furthermore, dysregulation of mitochondrial function and pH homeostasis, in which CA10 plays a role, have been linked to neurodegenerative diseases, cancer, and cardiovascular disorders. Elucidating the precise contributions of CA10 in these pathologies is an area of active investigation.

      Therapeutic Potential of Carbonic Anhydrase X:

      The unique properties and expression patterns of CA10 make it an intriguing target for therapeutic interventions. Modulating CA10 activity or expression could have implications in metabolic disorders, where the manipulation of mitochondrial function and pH regulation could offer therapeutic benefits. Developing selective inhibitors or activators of CA10 could be explored to regulate its enzymatic activity and modulate mitochondrial metabolism.

      Challenges and Future Directions:

      Although CA10 shows promise as a therapeutic target, several challenges remain. The elucidation of the precise regulatory mechanisms and signaling pathways involving CA10 within mitochondria is necessary for a comprehensive understanding of its function. Additionally, the development of specific modulators that selectively target CA10 without affecting other CAs or disrupting physiological processes is a critical consideration.

      Conclusion:

      The study of CA10 protein provides valuable insights into its distinct role in mitochondrial metabolism and disease pathogenesis. Understanding the molecular mechanisms and functional implications of CA10 opens avenues for the development of targeted therapies for metabolic disorders, neurodegenerative diseases, cancer, and cardiovascular disorders. Further research on CA10, its interactions, and its modulation in pathological conditions will contribute to the development of novel therapeutic interventions to improve patient outcomes.

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    Ca10 Human
  • View Data Sheet

    Name :

    RCN2 Human

    Description:

    Reticulocalbin 2 Human Recombinant

    Reticulocalbin-2, Calcium-binding protein ERC-55, E6-binding protein, 6BP, RCN2, ERC55, E6BP, ERC-55, TCBP49.

    Product # :

    PRO-189

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    Description

    RCN2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 313 amino acids (26-317 a.a.) and having a molecular mass of 36.8kDa (Molecular weight on SDS-PAGE will appear higher).RCN2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RCN2 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Reticulocalbin-2 (RCN2) is a member of the CREC protein family. RCN2 is a calcium-binding protein found in the lumen of the ER. RCN2 contains 6 conserved regions with similarity to a high affinity Ca(+2)-binding motif, the EF-hand.

    • Synonyms

      Reticulocalbin-2, Calcium-binding protein ERC-55, E6-binding protein, 6BP, RCN2, ERC55, E6BP, ERC-55, TCBP49.

    • 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 MEELHYPLGE RRSDYDREAL LGVQEDVDEY VKLGHEEQQK RLQAIIKKID LDSDGFLTES ELSSWIQMSF KHYAMQEAKQ QFVEYDKNSD DTVTWDEYNI QMYDRVIDFD ENTALDDAEE ESFRKLHLKD KKRFEKANQD SGPGLSLEEF IAFEHPEEVD
      YMTEFVIQEA LEEHDKNGDG FVSLEEFLGD YRWDPTANED PEWILVEKDR FVNDYDKDND GRLDPQELLP WVVPNNQGIA QEEALHLIDE MDLNGDKKLS EEEILENPDL FLTSEATDYG RQLHDDYFYH DEL.

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    Rcn2 Human
  • View Data Sheet

    Name :

    RCAN2 Human

    Description:

    Regulator of Calcineurin 2 Human Recombinant

    Regulator of calcineurin 2, DSCR1L1, MCIP2, Down syndrome critical region gene 1-like 1, ZAKI4, Myocyte-enriched calcineurin-interacting protein 2, Thyroid hormone-responsive protein ZAKI-4, CSP2, RCN2, thyroid hormone-responsive (skin fibroblasts).

    Product # :

    PRO-990

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    Description

    RCAN2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids (1-197 a.a.) and having a molecular mass of 24.1kDa.RCAN2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    RCAN2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 200mM NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

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    • Introduction

      RCAN2 is a member of the RCAN (Regulator of calcineurin) family that controls the activity of Calcineurin using a valine-rich region placed in their carboxyl tail. RCANs race against NFAT (nuclear factor of activated T-cells) to bind to the same docking site in calcineurin, and consequently inhibits or activates calcineurin activity. RCAN2 is a Ca(2+) dependent protein phosphatase which takes part in numerous neuornal functions.

    • Synonyms

      Regulator of calcineurin 2, DSCR1L1, MCIP2, Down syndrome critical region gene 1-like 1, ZAKI4, Myocyte-enriched calcineurin-interacting protein 2, Thyroid hormone-responsive protein ZAKI-4, CSP2, RCN2, thyroid hormone-responsive (skin fibroblasts).

    • 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 MPAPSMDCDV STLVACVVDV EVFTNQEVKE KFEGLFRTYD DCVTFQLFKS FRRVRINFSN PKSAARARIE LHETQFRGKK LKLYFAQVQT PETDGDKLHL APPQPAKQFL ISPPSSPPVG WQPINDATPV LNYDLLYAVA KLGPGEKYEL HAGTESTPSV VVHVCDSDIE EEEDPKTSPK PKIIQTRRPG LPPSVSN

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    Rcan2 Human
  • View Data Sheet

    Name :

    S100A7A Human

    Description:

    S100 Calcium Binding Protein A7A Human Recombinant

    NICE-2, NICE2, Protein S100-A7A, S100A15, S100A7f, S100A7L1, S100 calcium-binding protein A15, S100 calcium-binding protein A7A, S100 calcium-binding protein A7-like 1, S100A7A.

    Product # :

    PRO-756

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    Description

    The S100A7A Human Recombinant is manufactured with N-terminal fusion of 9 amino acids His Tag. The S100A7A His -Tagged Fusion Protein is a 12.3kDa protein containing 109 amino acid residues and 9 additional amino acid residues - His Tag (underlined).

    Source

    Escherichia Coli.

    Formulation

    Filtered and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl pH-7.5.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      S100A7A takes part in epidermal differentiation and inflammation thus is significant for the pathogenesis of psoriasis and other diseases.

    • Synonyms

      NICE-2, NICE2, Protein S100-A7A, S100A15, S100A7f, S100A7L1, S100 calcium-binding protein A15, S100 calcium-binding protein A7A, S100 calcium-binding protein A7-like 1, S100A7A.

    • Stability

      Store lyophilized S100A7A Human recombinant at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted S100A7A 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 pyrogen free water to a working concentration of 0.5mg/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

      MMKHHHHHHASNT­QAERSIIG MIDMFHKYTG RDGKIEKPSL LTMMKENFPN FLSACDKKGI HYLATVFEKK DKNEDKKIDF SEFLSLLGDI AADYHKQSHG AAPCSGGSQ.

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    S100A7A Human
  • View Data Sheet

    Name :

    CAPNS1 Antibody

    Description:

    Calpain, Small Subunit 1, Mouse Anti Human

    Calpain Small Subunit 1, CAPN4, Calcium-Activated Neutral Proteinase Small Subunit, Calcium-Dependent Protease Small Subunit 1, Calpain Regulatory Subunit, CANP Small Subunit, CDPS, CSS1, Calcium-Dependent Protease Small Subunit, Calcium-Dependent Protease Small Subunit, Calpain 4 Small Subunit (30K), Calpain Small Polypeptide, Calpain Small Subunit 1, CALPAIN4, CANPS, CAPNS, CANP, CAPNS1.

    Product # :

    ANT-587

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    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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    • Introduction

      Calpain, Small Subunit 1 (CAPNS1) belongs to the calpain small subunit family. Calpains are a ubiquitous, well-conserved family of calcium-dependent, cysteine proteases, widely distributed in mammalian cells. Calpain families are implicated in neurodegenerative processes, considering that their activation can be triggered by calcium influx and oxidative stress. Calpains function as heterodimers, comprising a specific large catalytic subunit (calpain 1 subunit in Calpain I, and calpain 2 subunit in Calpain II), and a common small regulatory subunit encoded by the CAPNS1 gene. The CAPNS1 protein is vital for the stability and function of both calpain heterodimers, whose proteolytic activities influence numerous cellular functions including apoptosis, proliferation, migration, adhesion, and autophagy.

    • Synonyms

      Calpain Small Subunit 1, CAPN4, Calcium-Activated Neutral Proteinase Small Subunit, Calcium-Dependent Protease Small Subunit 1, Calpain Regulatory Subunit, CANP Small Subunit, CDPS, CSS1, Calcium-Dependent Protease Small Subunit, Calcium-Dependent Protease Small Subunit, Calpain 4 Small Subunit (30K), Calpain Small Polypeptide, Calpain Small Subunit 1, CALPAIN4, CANPS, CAPNS, CANP, CAPNS1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human CAPNS1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human CAPNS1 protein 84-268 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      PAT1D11AT.

    • Applications

      CAPNS1 antibody has been tested by ELISA, Western blot analysis, ICC/IF and Flow cytometry to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      CAPNS1 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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    Capns1 Antibody
  • View Data Sheet

    Name :

    CIB1 Human

    Description:

    Calcium and Integrin Binding 1 Human Recombinant

    Calcium and integrin-binding protein 1, Calmyrin, DNA-PKcs-interacting protein, Kinase-interacting protein, SNK-interacting protein 2-28, SIP2-28, CIB1, CIB, KIP, PRKDCIP.

    Product # :

    PKA-345

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    Description

    CIB1 Human Recombinant is a single, non-glycosylated polypeptide chain (aa 1-191) containing a total of 211 amino acids and having a molecular mass of 23 kDa.CIB1 is fused to a 20 a.a His-tag and it was purified by conventional column chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CIB1 protein solution (1mg/ml) contains 20mM Tris-HCl, pH-8 & 5mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      CIB1 (Calcium and integrin binding 1) is regulatory protein with 50% homology to calmodulin and calcineurin B, that encodes a member of the calcium-binding protein family. CIB1 interacts with DNA-dependent protein kinase and may play a role in kinase-phosphatase regulation of DNA end joining. Also CIB1 is widely expressed and binds to a number of effectors, such as integrin ?IIb, PAK1, and polo-like kinases, in different tissues.

    • Synonyms

      Calcium and integrin-binding protein 1, Calmyrin, DNA-PKcs-interacting protein, Kinase-interacting protein, SNK-interacting protein 2-28, SIP2-28, CIB1, CIB, KIP, PRKDCIP.

    • 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 0.1% HSA or BSA. Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGGSGSRLSK ELLAEYQDLT FLTKQEILLA HRRFCELLPQ EQRTVESSLR AQVPFEQILS LPELKANPFK ERICRVFSTS PAKDSLSFED FLDLLSVFSD TATPDIKSHY AFRIFDFDDD GTLNREDLSR LVNCLTGEGE DTRLSASEMK QLIDNILEES DIDRDGTINL SEFQHVISRS PDFASSFKIV L.

    • Patent Protected Countries

      The Sale of recombinant Human CIB1 by ProSpec is prohibited in the United States of America.

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    Cib1 Human
  • View Data Sheet

    Name :

    BDNF Human

    Description:

    Brain-Derived Neurotrophic Factor Human Recombinant

    Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

    Product # :

    CYT-207

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    • Activity

    Description

    BDNF Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 119 amino acids (and an N-terminal Met) and having a total molecular mass of 28kDa. BDNF Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized with 20mM PB and 400mM NaCl, pH 7.2.

    Purity

    BDNF is greater than 950% as determined SDS-PAGE.

    Biological Activity

    The activity was determined using Immobilized Human TrkB-His tag protein 2ug/ml (100 μl/well) for its binding to NHS-Biotin BDNF. The ED50 of was found to be ≤20ng/mL

    Activity

    bdnf activity - Product image 1

    More Info

    • Introduction

      BDNF promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. BDNF is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the cns. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (ltp), long-term depression (ltd), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.

    • Synonyms

      Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BDNF 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 BDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

    • Background

      Final Thoughts

      Although more research is needed on the safety and effectiveness of BDNF human recombinant, trials suggest that this laboratory-produced protein may be effective in managing and treating several neurological and psychiatric disorders. It's important for experts to stay up to date on the latest developments and research to learn more about potential risks and benefits.

      What is the molecular weight/Mw of BDNF Protein?
      BDNF Protein has a total Mw of 27kDa.

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

      What is the Purity of BDNF Protein?
      BDNF Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of BDNF Protein?
      The ED50, as determined by the dose-dependent induction of C6 cells proliferation, is 1.3-2µg/ml.

      What is the amino acid sequence of BDNF Protein?
      MHSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

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

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

    • Protein content

      BDNF quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.6 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of Brain-derived Neurotrophic Factor as a Reference Standard.

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    Bdnf Human
  • View Data Sheet

    Name :

    S100A16 Human

    Description:

    S100 Calcium Binding Protein A16 Human Recombinant

    Protein S100-A16, Aging-associated gene 13 protein, Protein S100-F, S100 calcium-binding protein A16, S100A16, S100F, AAG13, DT1P1A7, MGC17528.

    Product # :

    PRO-155

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    • More Info

    Description

    S100A16 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 123 amino acids (1-103 a.a.) and having a molecular mass of 13.9kDa.S100A16 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    S100A16 (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 40% glycerol and 0.2M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      S100A16 belongs to the S100 protein super family containing calcium-binding EF-hand motifs. S100 proteins are cell and tissue specific and are engaged in various intra and extracellular processes through interacting with specific target proteins. The S100A16 expression is astrocyte-specific. S100A16 accumulates within nucleoli and translocates to the cytoplasm in reaction to Ca(2+) stimulation. S100A16 physically interacts with tumor suppressor protein p53 (which is a known inhibitor of adipogenesis) as determined Immunoprecipitation analysis.

    • Synonyms

      Protein S100-A16, Aging-associated gene 13 protein, Protein S100-F, S100 calcium-binding protein A16, S100A16, S100F, AAG13, DT1P1A7, MGC17528.

    • 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 MSDCYTELEK AVIVLVENFY KYVSKYSLVK NKISKSSFRE MLQKELNHML SDTGNRKAAD KLIQNLDANH DGRISFDEYW TLIGGITGPI AKLIHEQEQQ SSS.

    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.

    S100A16 Human
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