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Search results

1000 results found for “crystallin”

Name

Description

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  • View Data Sheet

    Name :

    CRTAM Human

    Description:

    Cytotoxic and Regulatory T Cell Molecule Human Recombinant

    Cytotoxic and Regulatory T Cell Molecule, Class I MHC Restricted T Cell Associated Molecule, Class-I MHC-Restricted T-Cell-Associated Molecule, Class-I MHC-Restricted T Cell Associated Molecule, Cytotoxic and Regulatory T-Cell Molecule, CD355 Antigen, CD355.

    Product # :

    PRO-2247

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    Description

    CRTAM produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 278 amino acids (18-287 a.a.) and having a molecular mass of 31.0kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).CRTAM is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    CRTAM protein solution (1mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Cytotoxic and Regulatory T Cell Molecule, also known as CRTAM belongs to the immunoglobulin superfamily which complies with the structural characteristics of the JAM family and is phylogenetically more closely related to nectin-like proteins. CRTAM is implicated in epithelial cell adhesion. Furthermore, CRTAM interacts with CADM1 as well as promotes natural killer (NK) cell cytotoxicity.

    • Synonyms

      Cytotoxic and Regulatory T Cell Molecule, Class I MHC Restricted T Cell Associated Molecule, Class-I MHC-Restricted T-Cell-Associated Molecule, Class-I MHC-Restricted T Cell Associated Molecule, Cytotoxic and Regulatory T-Cell Molecule, CD355 Antigen, CD355.

    • 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

      SLTNHTETIT VEEGQTLTLK CVTSLRKNSS LQWLTPSGFT IFLNEYPALK NSKYQLLHHS ANQLSITVPN VTLQDEGVYK CLHYSDSVST KEVKVIVLAT PFKPILEASV IRKQNGEEHV VLMCSTMRSK PPPQITWLLG NSMEVSGGTL HEFETDGKKC NTTSTLIIHT YGKNSTVDCI IRHRGLQGRK LVAPFRFEDL VTDEETASDA LERNSLSSQD PQQPTSTVSV TEDSSTSEID KEEKEQTTQD PDLTTEANPQ YLGLARKKSG LEHHHHHH.

    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.

    Crtam Human
  • View Data Sheet

    Name :

    SCG3 Human

    Description:

    Secretogranin III Human Recombinant

    Secretogranin III, secretogranin-3, SGIII.

    Product # :

    PRO-1556

    Price :

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    Description

    SCG3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 472 amino acids (20-468) and having a molecular mass of 53.0kDa.SCG3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SCG3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SCG3 belongs to the chromogranin/secretogranin family of neuroendocrine secretory proteins. Though, the function of SCG3 is unknown, Granins operate as precursors for biologically active peptides. Several granins are known to serve as helper proteins in sorting and proteolytic processing of prohormones.

    • Synonyms

      Secretogranin III, secretogranin-3, SGIII.

    • 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 MGSFPKPGGS QDKSLHNREL SAERPLNEQI AEAEEDKIKK TYPPENKPGQ SNYSFVDNLN LLKAITEKEK IEKERQSIRS SPLDNKLNVE DVDSTKNRKL IDDYDSTKSG LDHKFQDDPD GLHQLDGTPL TAEDIVHKIA ARIYEENDRA VFDKIVSKLL NLGLITESQA HTLEDEVAEV LQKLISKEAN NYEEDPNKPT SWTENQAGKI PEKVTPMAAI QDGLAKGEND ETVSNTLTLT NGLERRTKTY SEDNFEELQY FPNFYALLKS IDSEKEAKEK ETLITIMKTL IDFVKMMVKY GTISPEEGVS YLENLDEMIA LQTKNKLEKN ATDNISKLFP APSEKSHEET DSTKEEAAKM EKEYGSLKDS TKDDNSNPGG KTDEPKGKTE AYLEAIRKNI EWLKKHDKKG NKEDYDLSKM RDFINKQADA YVEKGILDKE EAEAIKRIYS SL.

    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.

    Scg3 Human
  • View Data Sheet

    Name :

    DCTN2 (1-406) Human

    Description:

    Dynactin 2 (1-406 a.a.) Human Recombinant

    DCTN2, Dynactin 2 (P50), DCTN50, Dynactin Complex 50 KDa Subunit, 50 KDa Dynein-Associated Polypeptide, P50 Dynamitin, 50 KD Dynein-Associated Polypeptide, DYNAMITIN, HEL-S-77, RBP50, Dynactin Complex 50 KD Subunit, Dynactin Subunit 2, Epididymis Secretory Protein Li 77, DCTN-50.

    Product # :

    PRO-1820

    Price :

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    Description

    Dynactin 2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 429 amino acids (1-406 a.a) and having a molecular mass of 47.2kDa.DCTN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DCTN2 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0), 20% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      DCTN2 is a 50kDa subunit of dynactin, which is a macromolecular complex consisting of 10-11 subunits ranging in size from 22 to 150 kDa. Dynactin binds to both microtubules and cytoplasmic dynein. Dynactin is involved in a various cellular functions, including ER-to-Golgi transport, the centripetal movement of lysosomes and endosomes, spindle formation, chromosome movement, nuclear positioning, and axonogenesis. The DCTN2 subunit is present in 4-5 copies per dynactin molecule. DCTN2 is comprised of 3 short alpha-helical coiled-coil domains which mediate association with self or other dynactin subunits. DCTN2 interacts directly with the largest subunit (p150) of dynactin and is able to affix p150 in place. DCTN2 modulates cytoplasmic dynein binding to an organelle, and plays a part in prometaphase chromosome alignment and spindle organization during mitosis. DCTN2 is involved in anchoring microtubules to centrosomes. DCTN2 has a role in synapse formation during brain development.

    • Synonyms

      DCTN2, Dynactin 2 (P50), DCTN50, Dynactin Complex 50 KDa Subunit, 50 KDa Dynein-Associated Polypeptide, P50 Dynamitin, 50 KD Dynein-Associated Polypeptide, DYNAMITIN, HEL-S-77, RBP50, Dynactin Complex 50 KD Subunit, Dynactin Subunit 2, Epididymis Secretory Protein Li 77, DCTN-50.

    • 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 MGSMADPKYA DLPGIARNEP DVYETSDLPE DDQAEFDAFA QELEELTSTS VEHIIVNPNA AYDKFKDKRV GTKGLDFSDR IGKTKRTGYE SGEYEMLGEG LGVKETPQQK YQRLLHEVQE LTTEVEKIKT TVKESATEEK LTPVLLAKQL AALKQQLVAS HLEKLLGPDA AINLTDPDGA LAKRLLLQLE ATKNSKGGSG GKTTGTPPDS SLVTYELHSR PEQDKFSQAA KVAELEKRLT ELETAVRCDQ DAQNPLSAGL QGACLMETVE LLQAKVSALD LAVLDQVEAR LQSVLGKVNE IAKHKASVED ADTQSKVHQL YETIQRWSPI ASTLPELVQR LVTIKQLHEQ AMQFGQLLTH LDTTQQMIAN SLKDNTTLLT QVQTTMRENL ATVEGNFASI DERMKKLGK.

    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.

    Dctn2 1 406 Human
  • View Data Sheet

    Name :

    SERPINA3

    Description:

    Alpha-1 AntiChymotrypsin Human Recombinant

    Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, SERPINA3, AACT, A1ACT, GIG24, GIG25, MGC88254.

    Product # :

    PRO-750

    Price :

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    Description

    SERPINA3 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 421 amino acids (24-423 a.a.) and having a molecular mass of 47.6 kDa.The SERPINA3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SERPINA3 solution contains 20mM Tris-HCl buffer pH-8, 1mM DTT, and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Alpha 1 ACT is an early-stage acute-phase plasma protein and a serpin that preferentially inactivates chymotrypsin, cathepsin G, and chymase. Alpha-1-ACT, a serine protease inhibitor, is tightly associated with amyloid plaques in Alzheimer's disease (AD) and in normal aged human and monkey brain.
      Regulation of the serine proteases and serine protease inhibitors plays an important role in neuromuscular differentiation. Prostate specific antigen (PSA), a chymotrypsin-like serine protease, is predominantly complexed to Alpha-1-ACT.

    • Synonyms

      Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, SERPINA3, AACT, A1ACT, GIG24, GIG25, MGC88254.

    • 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 MHPNSPLDEE NLTQENQDRG THVDLGLASA NVDFAFSLYK QLVLKAPDKN VIFSPLSIST ALAFLSLGAH NTTLTEILKG LKFNLTETSE AEIHQSFQHL LRTLNQSSDE LQLSMGNAMF VKEQLSLLDR FTEDAKRLYG SEAFATDFQD SAAAKKLIND YVKNGTRGKI TDLIKDLDSQ TMMVLVNYIF FKAKWEMPFD PQDTHQSRFY LSKKKWVMVP MMSLHHLTIP YFRDEELSCT VVELKYTGNA SALFILPDQD KMEEVEAMLL PETLKRWRDS LEFREIGELY LPKFSISRDY NLNDILLQLG IEEAFTSKAD LSGITGARNL AVSQVVHKAV LDVFEEGTEA SAATAVKITL LSALVETRTI VRFNRPFLMI IVPTDTQNIF FMSKVTNPKQ A.

    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.

    Serpina3 Human Recombinant
  • View Data Sheet

    Name :

    CAMLG Human

    Description:

    Calcium Modulating Ligand Human Recombinant

    Calcium Modulating Ligand, Calcium-Modulating Cyclophilin Ligand, Calcium-Signal Modulating Cyclophilin Ligand, Cyclophilin B-Binding Protein, CAML.

    Product # :

    PRO-1612

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    Description

    CAMLG Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 212 amino acids (1-189) and having a molecular mass of 23.2kDa.CAMLG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CAMLG solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CAMLG binds to cyclophilin B and operates downstream of the TCR and upstream of calcineurin by causing an influx of calcium. CAMLG is an essential membrane protein that takes part in the calcium signal transduction pathway, connecting cyclophilin B to calcium signaling.

    • Synonyms

      Calcium Modulating Ligand, Calcium-Modulating Cyclophilin Ligand, Calcium-Signal Modulating Cyclophilin Ligand, Cyclophilin B-Binding Protein, CAML.

    • 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 MGSMESMAVA TDGGERPGVP AGSGLSASQR RAELRRRKLL MNSEQRINRI MGFHRPGSGA EEESQTKSKQ QDSDKLNSLS VPSVSKRVVL GDSVSTGTTD QQGGVAEVKG TQLGDKLDSF IKPPECSSDV NLELRQRNRG DLTADSVQRG SRHGLEQYLS RFEEAMKLRK QLISEKPSQE DGNTTEEFDS FR

    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.

    Camlg Human
  • View Data Sheet

    Name :

    CCL28 Human

    Description:

    Mucosae-Associated Epithelial Chemokine Human Recombinant (CCL28)

    MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.

    Product # :

    CHM-353

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    Description

    CCL28 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 108 amino acids and having a molecular mass of 12.3 kDa. The CCL28 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM PBS and 150mM NaCl.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Determined by its ability to chemoattract human lymphocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

    Citations

    More Info

    • Introduction

      CCL28 is part of the subfamily of small cytokine CC genes. CCL28 shows chemotactic activity for resting CD4 or CD8 T cells and eosinophils. CCL28 binds to chemokine receptors CCR3 and CCR10. CCL28 is involved in the physiology of extracutaneous epithelial tissues, including diverse mucosal organs. CCL28 mediates mucosal immunity in HIV exposure and infection. CCL28 is involved in the pathogenesis of inflammatory skin diseases.
      Human CCL28 cDNA encodes a 127 amino acid residue precursor protein with a putative 22 amino acid residue signal peptide that is cleaved to produce the 105 amino acid residue mature protein. Human and mouse CCL28 are highly conserved, sharing 83% amino acid identity in their mature regions. CCL28 shares the most homology with CCL27/CTACK. Human and mouse CCL28 RNA expression was found to be highest in normal and pathologic colon with the protein being expressed by epithelial cells. Human CCL28 RNA was also present in normal and asthmatic lung tissues.

    • Synonyms

      MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CCL28 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL28 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 CCL28 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SEAILPIASS CCTEVSHHIS RRLLERVNMC RIQRADGDCD LAAVILHVKR RRICVSPHNH TVKQWMKVQA AKKNGKGNVC HRKKHHGKRN SNRAHQGKHE TYGHKTPY.

    • Background

      What is the molecular weight/Mw of CCL28 HUMAN Protein?
      CCL28 HUMAN Protein has a total Mw of 12.3kDa.

      What is the source or expression system of CCL28 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL28 HUMAN Protein?
      CCL28 HUMAN Protein is > 97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL28 HUMAN Protein?
      Determined by its ability to chemoattract human lymphocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

      What is the amino acid sequence of CCL28 HUMAN Protein?
      SEAILPIASS CCTEVSHHIS RRLLERVNMC RIQRADGDCD LAAVILHVKR RRICVSPHNH TVKQWMKVQA AKKNGKGNVC HRKKHHGKRN SNRAHQGKHE TYGHKTPY.

      What applications can CCL28 HUMAN Protein be used in?
      CCL28 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL28 HUMAN Protein?
      The endotoxin level is minimal, CCL28 HUMAN 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.

    Ccl28 Human
  • View Data Sheet

    Name :

    CCL3L1 Human

    Description:

    LD78-beta (CCL3L1) Human Recombinant

    C-C motif chemokine 3-like 1, G0/G1 switch regulatory protein 19-2, LD78-beta(1-70), PAT 464.2, Small-inducible cytokine A3-like 1, Tonsillar lymphocyte LD78 beta protein, CCL3L1, D17S1718, G0S19-2, SCYA3L1, LD78, 464.2, SCYA3L, LD78BETA, MGC12815.

    Product # :

    CHM-263

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    Description

    CCL3L1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7.7kDa. The CCL3L1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The biological activity was determined by its ability to chemoattract human monocytes using a concentration range of 1.0-10.0 ng/ml.

    Citations

    More Info

    • Introduction

      CCL3L1 is a small cytokine that belongs to the CC chemokines. The CCL3L1 gene is one of several cytokine genes clustered on the q-arm of chromosome 17. CCL3L1 is involved in immunoregulatory and inflammatory processes. CCL3L1 binds to several chemokine receptors including CCBP2 and CCR5. CCR5 is a co-receptor for HIV, and binding of the CCL3L1 protein to CCR5 inhibits HIV entry.

    • Synonyms

      C-C motif chemokine 3-like 1, G0/G1 switch regulatory protein 19-2, LD78-beta(1-70), PAT 464.2, Small-inducible cytokine A3-like 1, Tonsillar lymphocyte LD78 beta protein, CCL3L1, D17S1718, G0S19-2, SCYA3L1, LD78, 464.2, SCYA3L, LD78BETA, MGC12815.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CCL3L1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL3L1 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 CCL3L1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APLAADTPTA CCFSYTSRQI PQNFIADYFE TSSQCSKPSV IFLTKRGRQV CADPSEEWVQ KYVSDLELSA.

    • Background

      What is the molecular weight/Mw of CCL3L1 HUMAN Protein?
      CCL3L1 HUMAN Protein has a total Mw of 7.7kDa.

      What is the source or expression system of CCL3L1 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL3L1 HUMAN Protein?
      CCL3L1 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL3L1 HUMAN Protein?
      The biological activity was determined by its ability to chemoattract human monocytes using a concentration range of 1.0-10.0 ng/ml.

      What is the amino acid sequence of CCL3L1 HUMAN Protein?
      APLAADTPTA CCFSYTSRQI PQNFIADYFE TSSQCSKPSV IFLTKRGRQV CADPSEEWVQ KYVSDLELSA.

      What applications can CCL3L1 HUMAN Protein be used in?
      CCL3L1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL3L1 HUMAN Protein?
      The endotoxin level is minimal, CCL3L1 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CCL3L1 HUMAN that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CCL3L1 HUMAN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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.

    Ccl3L1 Human
  • View Data Sheet

    Name :

    Vaspin Human, His

    Description:

    Vaspin Human Recombinant, His Tag

    Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.

    Product # :

    CYT-459

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    Description

    Vaspin Human Recombinant produced in E.Coli is a single, non-glycosylated, His Tag, polypeptide chain containing 415 amino acids and having a molecular mass of 47 kDa.The Vaspin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Vaspin in 20mM Tris pH-8, 0.2mM PMSF and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Vaspin (visceral adipose-specific SERPIN), a newly identified adipokine, which is a member of serine protease inhibitor family. Vaspin is also a unique insulin sensitizing adipocytokine in obesity. A recent publication indicates that induction of human vaspin mRNA expression in adipose tissue is regulated in a fat depot-specific manner and could be associated with parameters of obesity, insulin resistance, and glucose metabolism.

    • Synonyms

      Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Liquid Vaspin although stable at 10°C for 1 week, should be stored 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MLKPSFSPRN YKALSEVQGW KQRMAAKELA RQNMDLGFKL LKKLAFYNPG RNIFLSPLSI STAFSMLCLG AQDSTLDEIK QGFNFRKMPE KDLHEGFHYI IHELTQKTQD LKLSIGNTLF IDQRLQPQRK FLEDAKNFYS AETILTNFQN LEMAQKQIND FISQKTHGKI NNLIENIDPG TVMLLANYIF FRARWKHEFD PNVTKEEDFF LEKNSSVKVP MMFRSGIYQV GYDDKLSCTI LEIPYQKNIT AIFILPDEGK LKHLEKGLQV DTFSRWKTLL SRRVVDVSVP RLHMTGTFDL KKTLSYIGVS KIFEEHGDLT KIAPHRSLKV GEAVHKAELK MDERGTEGAA GTGAQTLPME TPLVVKIDKP YLLLIYSEKI PSVLFLGKIV NPIGK.

    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.

    Vaspin Human
  • View Data Sheet

    Name :

    Clusterin Human

    Description:

    Clusterin Human Recombinant

    CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.

    Product # :

    CYT-278

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    Description

    Clusterin Human Recombinant produced in HEK is a glycosylated, polypeptide chain containing 438 amino acids and having a molecular mass of 51.27 kDa. Clusterin (1-427 a.a.) is fused to 11 a.a. flag tag at c-terminal and purified by proprietary chromatographic techniques.

    Source

    293 cell line (Human embryonic kidney).

    Formulation

    Filtered (0.4 micron) and lyophilized PBS, pH 7.5.

    Purity

    Greater than 95% as determined by SDS PAGE.

    Citations

    More Info

    • Introduction

      Clusterin also named Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
      The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by five disulfide bridges and are flanked by two predicted coiled-coil a-helices and three predicted amphipathic a-helices.
      Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
      It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
      A genuine function of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced insults caused by degraded and misfolded protein precipitates.
      Clusterin is up- or down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others.

    • Synonyms

      CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.

    • Physical Appearance

      Filtered, White, Lyophilized 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

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

    • Amino Acid Sequence

      DQTVSDNELQ EMSNQGSKYV NKEIQNAVNG VKQIKTLIEK TNEERKTLLS NLEEAKKKKE DALNETRESE TKLKELPGVC NETMMALWEE CKPCLKQTCM KFYARVCRSGS GLVGRQLEE FLNQSSPFYF WMNGDRIDSL LENDRQQTHM LDVMQDHFSRA SSIIDELFQ DRFFTREPQD TYHYLPFSLP HRRPHFFFPK SRIVRSLMPF SPYEPLNFHA MFQPFLEMIH EAQQAMDIHF HSPAFQHPPT EFIREGDDDR TVCREIRHNS TGCLRMKDQC DKCREILSVD CSTNNPSQAKLRRELDESLQ VAERLTRKYN ELLKSYQWKM LNTSSLLEQL NEQFNWVSRL ANLTQGEDQYYLRVTTVASH TSDSDVPSGV TEVVVKLFDS DPITVTVPVE VSRKNPKFME TVAEKALQEY RKKHREEAAA DYKDDDDK.

    • Background

      What is the molecular weight/Mw of CLUSTERIN Protein?
      CLUSTERIN Protein has a total Mw of 51.27kDa.

      What is the source or expression system of CLUSTERIN Protein?
      293 cell line
      What is the Purity of CLUSTERIN Protein?
      CLUSTERIN Protein is >95% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of CLUSTERIN Protein?
      DQTVSDNELQ EMSNQGSKYV NKEIQNAVNG VKQIKTLIEK TNEERKTLLS NLEEAKKKKE DALNETRESE TKLKELPGVC NETMMALWEE CKPCLKQTCM KFYARVCRSGS GLVGRQLEE FLNQSSPFYF WMNGDRIDSL LENDRQQTHM LDVMQDHFSRA SSIIDELFQ DRFFTREPQD TYHYLPFSLP HRRPHFFFPK SRIVRSLMPF SPYEPLNFHA MFQPFLEMIH EAQQAMDIHF HSPAFQHPPT EFIREGDDDR TVCREIRHNS TGCLRMKDQC DKCREILSVD CSTNNPSQAKLRRELDESLQ VAERLTRKYN ELLKSYQWKM LNTSSLLEQL NEQFNWVSRL ANLTQGEDQYYLRVTTVASH TSDSDVPSGV TEVVVKLFDS DPITVTVPVE VSRKNPKFME TVAEKALQEY RKKHREEAAA DYKDDDDK.

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

      What is the endotoxin level for CLUSTERIN Protein?
      The endotoxin level is minimal, CLUSTERIN 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.

    Clusterin Human Recombinant
  • View Data Sheet

    Name :

    LGALS8 Human, His

    Description:

    Galectin-8 Human Recombinant, His Tag

    Gal-8, PCTA1, Po66-CBP, Prostate carcinoma tumor antigen 1.

    Product # :

    CYT-727

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    Description

    LGALS8 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 337 amino acids (1-317 a.a.) and having a molecular mass of 37.9 kDa. The LGALS8 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Galectin-8 His tag 0.5mg/ml protein solution contains 20mM Tris-HCl pH-8, 0.1M NaCl, 10% glycerol & 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 for this effect is 5–10ug/ml. Measured by its ability to agglutinate human red blood cells corresponding to a specific activity of 100-200IU/mg.

    SDS-PAGE

    LGALS8 Human, His-SDS-PAGE - Product image 1

    Citations

    More Info

    • Introduction

      LGALS8 is a prostate-specific antigen that is solely overexpressed in malignant tumors and thus is a supplementary specific identifier of malignancies. LGALS8 is part of the galectin gene family which facilitates both cell-cell and cell matrix interactions in a method parallel to the selectin subgroup of C-type lectins.

    • Synonyms

      Gal-8, PCTA1, Po66-CBP, Prostate carcinoma tumor antigen 1.

    • 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 MMLSLNNLQN IIYNPVIPFV GTIPDQLDPG TLIVIRGHVP SDADRFQVDL QNGSSMKPRA DVAFHFNPRF
      KRAGCIVCNT LINEKWGREE ITYDTPFKRE KSFEIVIMVL KDKFQVAVNG KHTLLYGHRI GPEKIDTLGI YGKVNIHSIG FSFSSDLQST
      QASSLELTEI SRENVPKSGT PQLRLPFAAR LNTPMGPGRT VVVKGEVNAN AKSFNVDLLA GKSKDIALHL NPRLNIKAFV RNSFLQESWG
      EEERNITSFP FSPGMYFEMI IYCDVREFKV AVNGVHSLEY KHRFKELSSI DTLEINGDIH LLEVRSW.

    • Background

      What is the molecular weight/Mw of LGALS8 HUMAN, HIS Protein?
      LGALS8 HUMAN, HIS Protein has a total Mw of 37.9kDa.

      What is the source or expression system of LGALS8 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of LGALS8 HUMAN, HIS Protein?
      LGALS8 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of LGALS8 HUMAN, HIS Protein?
      The ED50 for this effect is 5–10ug/ml. Measured by its ability to agglutinate human red blood cells corresponding to a specific activity of 100-200IU/mg.What is the amino acid
      sequence of LGALS8 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MMLSLNNLQN IIYNPVIPFV GTIPDQLDPG TLIVIRGHVP SDADRFQVDL QNGSSMKPRA DVAFHFNPRF
      KRAGCIVCNT LINEKWGREE ITYDTPFKRE KSFEIVIMVL KDKFQVAVNG KHTLLYGHRI GPEKIDTLGI YGKVNIHSIG FSFSSDLQST
      QASSLELTEI SRENVPKSGT PQLRLPFAAR LNTPMGPGRT VVVKGEVNAN AKSFNVDLLA GKSKDIALHL NPRLNIKAFV RNSFLQESWG
      EEERNITSFP FSPGMYFEMI IYCDVREFKV AVNGVHSLEY KHRFKELSSI DTLEINGDIH LLEVRSW.

      What applications can LGALS8 HUMAN, HIS Protein be used in?
      LGALS8 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for LGALS8 HUMAN, HIS Protein?
      The endotoxin level is minimal, LGALS8 HUMAN, HIS 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.

    Lgals8 Human His
  • View Data Sheet

    Name :

    CRABP2 Human

    Description:

    Cellular Retinoic Acid binding Protein 2 Human Recombinant

    RBP6, CRABP-II, CRABP2, RETINOIC ACID-BINDING PROTEIN CELLULAR TYPE II, Cellular retinoic acid-binding protein 2, Cellular retinoic acid-binding protein II.

    Product # :

    PRO-637

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    Description

    CRABP2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 136 amino acids and having a molecular mass of 15.6 kDa. The CRABP2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CRABP2 protein solution contains 20mM Tris-HCl pH-8 and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CRABP2 NCBI Accession No: NP_001869 regulates the access of retinoic acid to the nuclear retinoic acid receptors. CRABP2 is involved in a regulatory feedback mechanism that controls the action of retinoic acid on cell differentiation.
      CRABP2 is involved in the conversion of vitamin A into its intracellular active form retinoic acid, which regulate the genes responsible for lipid metabolism and adipocyte differentiation. CRABP2 gene is located on chromosome 1q21-23 and this region has been linked with related disorders such as familial combined hyperlipidemia (FCHL) and type 2 diabetes mellitus.
      CRABP proteins are of low molecular weight having an important function in retinoic acid-mediated regulation of human skin growth and differentiation.

    • Synonyms

      RBP6, CRABP-II, CRABP2, RETINOIC ACID-BINDING PROTEIN CELLULAR TYPE II, Cellular retinoic acid-binding protein 2, Cellular retinoic acid-binding protein II.

    • 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

      MPNFSGNWKI IRSENFEELL KVLGVNVMLR KIAVAAASKP AVEIKQEGDT FYIKTSTTVR TTEINFKVGE EFEEQTVDGR PCKSLVKWES ENKMVCEQKL LKGEGPKTSW TRELTNDGEL ILTMTADDVV CTRVYVRE.

    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.

    Crabp2 Human
  • View Data Sheet

    Name :

    SERPINI1 Human, His

    Description:

    Serpin Peptidase Inhibitor, Clade I Member 1 Human Recombinant, His Tag

    Neuroserpin, Peptidase inhibitor 12, PI-12, Serpin I1, SERPINI1, PI12.

    Product # :

    PRO-1595

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    Description

    SERPINI1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 17-410) containing 404 amino acids and including a 10 a.a N-terminal His tag. The total molecular mass is 45.9kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4 µm) and lyophilized from 0.5mg/ml in 0.025M phosphate buffer and 0.035M NaCl, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SERPINI1 (Neuroserpin) is an inhibitory serpin which is expressed primarily in the central nervous system. Even though the physiological target of SERPINI1 is still vague, amassed evidence suggest that SERPINI1 has an imperative role in controlling proteolytic degradation of extracellular matrix (ECM) during synaptogenesis and the subsequent development of neuronal plasticity. The neuroprotective role of SERPINI1 has been demonstrated in transgenic mice lacking SERPINI1 expression. The deficiency of SERPINI1 in these mice is linked with motor neuron disease characterized by axonal degradation. In humans, defects in SERPINI1, caused by point mutations in the neuroserpin gene, trigger a hereditary disorder known as the familial encephalopathy with neuroserpin inclusion bodies (FENIB).

    • Synonyms

      Neuroserpin, Peptidase inhibitor 12, PI-12, Serpin I1, SERPINI1, PI12.

    • 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. SERPINI1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASTGATFPEEAI ADLSVNMYNR LRATGEDENI LFSPLSIALA MGMMELGAQG STQKEIRHSM GYDSLKNGEE FSFLKEFSNM VTAKESQYVM KIANSLFVQN GFHVNEEFLQ MMKKYFNAAV NHVDFSQNVA VANYINKWVE NNTNNLVKDL VSPRDFDAAT YLALINAVYF KGNWKSQFRP ENTRTFSFTK DDESEVQIPM MYQQGEFYYG EFSDGSNEAG GIYQVLEIPY EGDEISMMLV LSRQEVPLAT LEPLVKAQLV EEWANSVKKQ KVEVYLPRFT VEQEIDLKDV LKALGITEIF IKDANLTGLS DNKEIFLSKA IHKSFLEVNE EGSEAAAVSG MIAISRMAVL YPQVIVDHPF FFLIRNRRTG TILFMGRVMH PETMNTSGHD FEEL.

    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.

    Serpini1 Human His
  • View Data Sheet

    Name :

    EFNB1 Human, Sf9

    Description:

    Ephrin-B1 Human Recombinant, Sf9

    Ephrin B1, ELK Ligand, Ephrin-B1, Elk-L, EPLG2, LERK2, EFL3, Craniofrontonasal Syndrome (Craniofrontonasal Dysplasia), Eph-Related Receptor Tyrosine Kinase Ligand 2, EPH-Related Receptor Tyrosine Kinase Ligand 2, LERK-2, EFL-3, CFND, EFB1, CFNS, ELK ligand, ELK-L, EPH-related receptor tyrosine kinase ligand 2. 

    Product # :

    PRO-2543

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    Description

    EFNB1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 452 amino acids (28-237a.a.) and having a molecular mass of 50.3kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).EFNB1 is expressed with a 242 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    EFNB1 protein solution (1mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      EFNB1 is a member of the Eph family. The cell-surface proteins Ephrins split into two groups, ephrin-A and ephrin-B, based on their structure and function and perform as ligands for Eph receptors. The transmembrane EFNB1 proteins have conserved cytoplasmic tyrosine residues that are phosphorylated upon interaction with an EphB receptor. In addition, EFNB1 transduces outside-in signals by C-terminal protein interfaces which influence integrin-mediated cell attachment and migration.

    • Synonyms

      Ephrin B1, ELK Ligand, Ephrin-B1, Elk-L, EPLG2, LERK2, EFL3, Craniofrontonasal Syndrome (Craniofrontonasal Dysplasia), Eph-Related Receptor Tyrosine Kinase Ligand 2, EPH-Related Receptor Tyrosine Kinase Ligand 2, LERK-2, EFL-3, CFND, EFB1, CFNS, ELK ligand, ELK-L, EPH-related receptor tyrosine kinase ligand 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

      ADPLAKNLEP VSWSSLNPKF LSGKGLVIYP KIGDKLDIIC PRAEAGRPYE YYKLYLVRPE QAAACSTVLD PNVLVTCNRP EQEIRFTIKF QEFSPNYMGL EFKKHHDYYI TSTSNGSLEG LENREGGVCR TRTMKIIMKV GQDPNAVTPE QLTTSRPSKE ADNTVKMATQ APGSRGSLGD
      SDGKHETVNQ EEKSGPGASG GSSGDPDGFF NSKLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN
      QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.

    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.

    Ephrin B1
  • View Data Sheet

    Name :

    PFN2 Human

    Description:

    Profilin-2 Human Recombinant

    Profilin-II, PFN2, Profilin-2, PFL, D3S1319E.

    Product # :

    PRO-809

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    Description

    PFN2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids (1-140 a.a.) and having a molecular mass of 17.2 kDa. PFN2 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    PFN2 protein solution (1mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      PFN2 is a ubiquitous actin monomer-binding protein which is part of the profilin family. PFN2 regulates actin polymerization in response to extra cellular signals. PFN2 binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, while it increases it at low concentrations. PFN2 binds to PIP2, it inhibits the formation of IP3 and DG.

    • Synonyms

      Profilin-II, PFN2, Profilin-2, PFL, D3S1319E.

    • 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 MAGWQSYVDN LMCDGCCQEA AIVGYCDAKY VWAATAGGVF QSITPIEIDM IVGKDREGFF TNGLALGAKK CSVIRDSLYV DGDCTMDIRT KSQGGEPTYN VAVGRAGRVL VFVMGKEGVH GGGLNKKAYS MAKYLRDSGF.

    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.

    Pfn2 Human
  • View Data Sheet

    Name :

    CDH2 Human

    Description:

    Cadherin 2 Human Recombinant

    Cadherin 2, Cadherin 2, Type 1, N-Cadherin (Neuronal), Neural Cadherin, N-Cadherin, CDw325, NCAD, CDHN, Calcium-Dependent Adhesion Protein, Neuronal, CD325 Antigen, N-Cadherin 1, Cadherin-2, CD325.

    Product # :

    PRO-2455

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    Description

    CDH2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 574 amino acids (160-724a.a.) and having a molecular mass of 62.9kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).CDH2 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CDH2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Cadherin-2 isoform 1, also known as CDH2 is a transmembrane, homophilic glycoprotein which belongs to the calcium-dependent cell adhesion molecule family. CDH2 takes part in neurons and later on was discovered to participate in cardiac muscle and in cancer metastasis as well. The CDH2 loss promotes tumorigenesis through releasing membrane-bound β-catenin, and so stimulating Wnt signaling. Furthermore, CDH2 appears to be implicated in tumor development, however this discovery is limited in adrenocortical tumors-ACTs.

    • Synonyms

      Cadherin 2, Cadherin 2, Type 1, N-Cadherin (Neuronal), Neural Cadherin, N-Cadherin, CDw325, NCAD, CDHN, Calcium-Dependent Adhesion Protein, Neuronal, CD325 Antigen, N-Cadherin 1, Cadherin-2, CD325.

    • 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

      ADPDWVIPPI NLPENSRGPF PQELVRIRSD RDKNLSLRYS VTGPGADQPP TGIFIINPIS GQLSVTKPLD REQIARFHLR AHAVDINGNQ VENPIDIVIN VIDMNDNRPE FLHQVWNGTV PEGSKPGTYV MTVTAIDADD PNALNGMLRY RIVSQAPSTP SPNMFTINNE TGDIITVAAG LDREKVQQYT LIIQATDMEG NPTYGLSNTA TAVITVTDVN DNPPEFTAMT FYGEVPENRV DIIVANLTVT DKDQPHTPAW NAVYRISGGD PTGRFAIQTD PNSNDGLVTV VKPIDFETNR MFVLTVAAEN QVPLAKGIQH PPQSTATVSV TVIDVNENPY FAPNPKIIRQ EEGLHAGTML TTFTAQDPDR YMQQNIRYTK LSDPANWLKI DPVNGQITTI AVLDRESPNV KNNIYNATFL ASDNGIPPMS GTGTLQIYLL DINDNAPQVL PQEAETCETP DPNSINITAL DYDIDPNAGP FAFDLPLSPV TIKRNWTITR LNGDFAQLNL KIKFLEAGIY EVPIIITDSG NPPKSNISIL RVKVCQCDSN GDCTDVDRIV GAGLGTGAHH HHHH.

    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.

    Cdh2 Human
  • View Data Sheet

    Name :

    S100A7 Human

    Description:

    S100 Calcium Binding Protein A7 Human Recombinant

    S100 calcium-binding protein A7 (psoriasin 1), S100A7c, PSOR1.

    Product # :

    PRO-149

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    Description

    S100A7 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 13.6 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

    S100A7 protein at 0.5mg/ml in 20mM Tris-HCl, pH-8, 0.1M NaCl, 1mM DTT and 30% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      S100A7 is a member of the S-100 family of calcium binding proteins and is produced through a non-classical secretory pathway to the cytoplasm. S100A7 takes part in the regulation of several cellular courses, such as cell cycle, cell progression and cellular differentiation. S100A7 holds two EF-hand domains and is extremely upregulated in psoriatic epidermis, in addition to bladder squamous cell carcinoma and breast cancer tissue, signifying a probable part in carcinogenesis.

    • Synonyms

      S100 calcium-binding protein A7 (psoriasin 1), S100A7c, PSOR1.

    • 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 MSNTQAERSI IGMIDMFHKY TRRDDKIDKP SLLTMMKENFPNFLSACDKK GTNYLADVFE KKDKNEDKKI DFSEFLSLLG DIATDYHKQS HGAAPCSGGS Q.

    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.

    S100A7 Human
  • View Data Sheet

    Name :

    CYTH2 Human

    Description:

    Cytohesin 2 Human Recombinant

    ARF Nucleotide-Binding Site Opener, Pleckstrin Homology Sec7 And Coiled-Coil Domains 2 (Cytohesin-2), PH SEC7 And Coiled-Coil Domain-Containing Protein 2, Cytohesin 2, Protein ARNO, ARF Exchange Factor, Sec7p-Like, PSCD2, PSCD2L, CTS18.1, Sec7p-L, SEC7L.

    Product # :

    PRO-1248

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    Description

    CYTH2 Human Recombinant produced in E. coli is a single polypeptide chain containing 422 amino acids (1-399) and having a molecular mass of 48.9 kDa. CYTH2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CYTH2 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Cytohesin 2 (CYTH2) is an ARF-1 guanine nucleotide exchange factor (GEF). ARF (ADP ribosylation factor) proteins are a part of a group within the RAS superfamily and bindes GTP-b proteins central to the process of vesicle budding. CYTH2 promotes guanine-nucleotide exchange on ARF1, ARF3 and ARF6. Furthermore, CYTH2 promotes the activation of ARF factors through replacement of GDP with GTP. The protein encoded by CYTH2 is a member of the PSCD family. Members of PSCD family appear to mediate the regulation of protein sorting and membrane trafficking. The cell membrane form, in association with ARL4 proteins, recruits ARF6 to the plasma membrane.

    • Synonyms

      ARF Nucleotide-Binding Site Opener, Pleckstrin Homology Sec7 And Coiled-Coil Domains 2 (Cytohesin-2), PH SEC7 And Coiled-Coil Domain-Containing Protein 2, Cytohesin 2, Protein ARNO, ARF Exchange Factor, Sec7p-Like, PSCD2, PSCD2L, CTS18.1, Sec7p-L, SEC7L.

    • 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 MGSMEDGVYE PPDLTPEERM ELENIRRRKQ ELLVEIQRLR EELSEAMSEV EGLEANEGSK TLQRNRKMAM GRKKFNMDPK KGIQFLVENE LLQNTPEEIA RFLYKGEGLN KTAIGDYLGE REELNLAVLH AFVDLHEFTD LNLVQALRQF LWSFRLPGEA QKIDRMMEAF AQRYCLCNPG VFQSTDTCYV LSFAVIMLNT SLHNPNVRDK PGLERFVAMN RGINEGGDLP EELLRNLYDS IRNEPFKIPE DDGNDLTHTF FNPDREGWLL KLGGRVKTWK RRWFILTDNC LYYFEYTTDK EPRGIIPLEN LSIREVDDPR KPNCFELYIP NNKGQLIKAC KTEADGRVVE GNHMVYRISA PTQEEKDEWI KSIQAAVSVD PFYEMLAARK KRISVKKKQE QP.

    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.

    Cyth2 Human
  • View Data Sheet

    Name :

    STX11 Human

    Description:

    Syntaxin-11 Human Recombinant

    Syntaxin-11, STX11, FHL4, HLH4, HPLH4.

    Product # :

    PRO-1111

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    Description

    STX11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 311 amino acids (1-287 a.a) and having a molecular mass of 35.8kDa.STX11 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    STX11 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Syntaxin-11 (STX11) belongs to the t-SNARE family. Syntaxin-11 regulates protein transport between late endosomes and the trans-Golgi network. STX11 interacts with the SNARE proteins SNAP-23 and VAMP. STX11 gene mutations are linked with familial hemophagocytic lymphohistiocytosis.

    • Synonyms

      Syntaxin-11, STX11, FHL4, HLH4, HPLH4.

    • 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 MGSHMKDRLA ELLDLSKQYD QQFPDGDDEF DSPHEDIVFE TDHILESLYR DIRDIQDENQ LLVADVKRLG KQNARFLTSM RRLSSIKRDT NSIAKAIKAR GEVIHCKLRA MKELSEAAEA QHGPHSAVAR ISRAQYNALT LTFQRAMHDY NQAEMKQRDN CKIRIQRQLE IMGKEVSGDQ IEDMFEQGKW DVFSENLLAD VKGARAALNE IESRHRELLR LESRIRDVHE LFLQMAVLVE KQADTLNVIE LNVQKTVDYT GQAKAQVRKA VQYEEKNPCR TLCCFCCPCL 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.

    Stx11 Human
  • View Data Sheet

    Name :

    CALR Human

    Description:

    Calreticulin Human Recombinant

    cC1qR, CRT, FLJ26680, RO, SSA, CRP55, Calreticulin, ERp60, CRTC, CALR.

    Product # :

    PRO-813

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    Description

    CALR Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 421 amino acids (18-417 a.a.) and having a molecular mass of 48.7 kDa. CALR protein is fused to a 21 amino acid His-Tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    CALR Human solution containing 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CALR is a multifunctional protein that acts as a main Ca(2+)-binding (storage) protein in the lumen of the endoplasmic reticulum. Calreticulin is localized in the nucleus, and participates in transcription regulation. Calreticulin binds to the synthetic peptide KLGFFKR, which is nearly identical to an amino acid sequence in the DNA-binding domain of the superfamily of nuclear receptors. CALR binds to antibodies in specific sera of systemic lupus and Sjogren patients which have anti-Ro/SSA antibodies, it is well conserved among species, and it is positioned in the endoplasmic and sarcoplasmic reticulum where it binds calcium. The amino terminus of CALR interacts with the DNA-binding domain of the glucocorticoid receptor and prevents the receptor from binding to its specific glucocorticoid response element. CALR reduces the binding of androgen receptor to its hormone-responsive DNA element and inhibits androgen receptor and retinoic acid receptor transcriptional activities in vivo, as well as retinoic acid-induced neuronal differentiation. Therefore, CALR acts as a significant modulator of the regulation of gene transcription by nuclear hormone receptors.

    • Synonyms

      cC1qR, CRT, FLJ26680, RO, SSA, CRP55, Calreticulin, ERp60, CRTC, CALR.

    • 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 MEPAVYFKEQ FLDGDGWTSR WIESKHKSDF GKFVLSSGKF YGDEEKDKGL QTSQDARFYA LSASFEPFSN KGQTLVVQFT VKHEQNIDCG GGYVKLFPNS LDQTDMHGDS EYNIMFGPDI CGPGTKKVHV IFNYKGKNVL INKDIRCKDD EFTHLYTLIV RPDNTYEVKI DNSQVESGSL EDDWDFLPPK KIKDPDASKP EDWDERAKID DPTDSKPEDW DKPEHIPDPD AKKPEDWDEE MDGEWEPPVI QNPEYKGEWK PRQIDNPDYK GTWIHPEIDN PEYSPDPSIY AYDNFGVLGL DLWQVKSGTI FDNFLITNDE AYAEEFGNET WGVTKAAEKQ MKDKQDEEQR LKEEEEDKKR KEEEEAEDKE DDEDKDEDEE DEEDKEEDEE EDVPGQAKDE L.

    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.

    Calr Human
  • View Data Sheet

    Name :

    FHIT Human

    Description:

    Fragile Histidine Triad Human Recombinant

    EC 3.6.1.29, Dinucleosidetriphosphatase, Bis (5''-adenosyl)-triphosphatase , AP3Aase, AP3A hydrolase, Diadenosine 5'',5''''''-P1,P3-triphosphate hydrolase, FRA3B.

    Product # :

    PRO-828

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    Description

    FHIT Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 155 amino acids (1-147 a.a.) and having a molecular mass of 17.9 kDa. FHIT protein is fused to an 8 amino acid His tag at C-terminus and is purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    FHIT Human solution containing 20mM Tris-HCl pH-8 & 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      FHIT enzyme cleaves adenosine 5'' PPP 5'' A to yield AMP and ADP. FHIT gene includees the regular fragile site FRA3B on chromosome 3. Alterations and deletions of the FHIT gene are highly linked to the genesis and establishment of human tumors of the lung, cervix, breast, colon, stomach and pancreas. In normal cells, FHIT functions as a tumor suppressor and physically relates with ubiquitin conjugating enzyme 9.

    • Synonyms

      EC 3.6.1.29, Dinucleosidetriphosphatase, Bis (5''-adenosyl)-triphosphatase , AP3Aase, AP3A hydrolase, Diadenosine 5'',5''''''-P1,P3-triphosphate hydrolase, FRA3B.

    • 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

      MSFRFGQHLI KPSVVFLKTE LSFALVNRKP VVPGHVLVCP LRPVERFHDL RPDEVADLFQ TTQRVGTVVE KHFHGTSLTF SMQDGPEAGQ TVKHVHVHVL PRKAGDFHRN DSIYEELQKH DKEDFPASWR SEEEMAAEAA ALRVYFQLEH HHHHH.

    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.

    Fhit Human
  • View Data Sheet

    Name :

    GCLM Human

    Description:

    Glutamate-Cysteine Ligase, Modifier Subunit Human Recombinant

    Glutamate--cysteine ligase regulatory subunit, GCS light chain, Gamma-ECS regulatory subunit, Gamma-glutamylcysteine synthetase regulatory subunit, Glutamate--cysteine ligase modifier subunit, GCLM, GLCLR.

    Product # :

    ENZ-636

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    Description

    GCLM Human Recombinant produced in E. coli is a single polypeptide chain containing 298 amino acids (1-274) and having a molecular mass of 33.3kDa.GCLM is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GCLM solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.15M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Glutamate-cysteine ligase (GCLM) is the first rate limiting enzyme of glutathione synthesis. The GCLM enzyme is comprised of 2 subunits, a heavy catalytic subunit and a light regulatory subunit. GCLM deficiency is associated with some forms of hemolytic anemia.

    • Synonyms

      Glutamate--cysteine ligase regulatory subunit, GCS light chain, Gamma-ECS regulatory subunit, Gamma-glutamylcysteine synthetase regulatory subunit, Glutamate--cysteine ligase modifier subunit, GCLM, GLCLR.

    • 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 MGSHMGTDSR AAKALLARAR TLHLQTGNLL NWGRLRKKCP STHSEELHDC IQKTLNEWSS QINPDLVREF PDVLECTVSH AVEKINPDER EEMKVSAKLF IVESNSSSST RSAVDMACSV LGVAQLDSVI IASPPIEDGV NLSLEHLQPY WEELENLVQS KKIVAIGTSD LDKTQLEQLY QWAQVKPNSN QVNLASCCVM PPDLTAFAKQ FDIQLLTHND PKELLSEASF QEALQESIPD IQAHEWVPLW LLRYSVIVKS RGIIKSKGYI LQAKRRGS.

    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.

    Gclm Human
  • View Data Sheet

    Name :

    Vaspin Human

    Description:

    Vaspin Recombinant Human

    Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.

    Product # :

    CYT-1132

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    Description

    Vaspin Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 394 amino acids and having a molecular mass of 45.1kDa. Vaspin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in 20mM Tris-HCl, pH 8.0, 150mM NaCl and 0.02 % Tween-20.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Vaspin (visceral adipose-specific SERPIN) is a newly identified adipokine, which is a member of serine protease inhibitor family. Vaspin is also a unique insulin sensitizing adipocytokine in obesity. A recent publication indicates that induction of human vaspin mRNA expression in adipose tissue is regulated in a fat depot-specific manner and could be associated with parameters of obesity, insulin resistance, and glucose metabolism.

    • Synonyms

      Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      LKPSFSPRNY KALSEVQGWK QRMAAKELAR QNMDLGFKLL KKLAFYNPGR NIFLSPLSIS TAFSMLCLGA QDSTLDEIKQ GFNFRKMPEK DLHEGFHYII HELTQKTQDL KLSIGNTLFI DQRLQPQRKF LEDAKNFYSA ETILTNFQNL EMAQKQINDF ISQKTHGKIN NLIENIDPGT VMLLANYIFF RARWKHEFDP NVTKEEDFFL EKNSSVKVPM MFRSGIYQVG YDDKLSCTIL EIPYQKNITA IFILPDEGKL KHLEKGLQVD TFSRWKTLLS RRVVDVSVPR LHMTGTFDLK KTLSYIGVSK IFEEHGDLTK IAPHRSLKVG EAVHKAELKM DERGTEGAAG TGAQTLPMET PLVVKIDKPY LLLIYSEKIP SVLFLGKIVN PIGK.

    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.

    Vaspin Protein
  • View Data Sheet

    Name :

    CCL7 Human

    Description:

    Monocyte Chemotactic Protein-3 Human Recombinant (CCL7)

    Small inducible cytokine A7, CCL7, Monocyte chemotactic protein 3, MCP-3, Monocyte chemoattractant protein 3, NC28, chemokine (C-C motif) ligand 7, FIC, MARC, MCP3, SCYA6, SCYA7, MGC138463, MGC138465.

    Product # :

    CHM-317

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    Description

    Monocyte Chemotactic Protein-3 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 76 amino acids and having a molecular mass of 9011 Dalton. The MCP-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The specific activity as determined by the ability of MCP-3 to chemoattract human peripheral blood at 8 - 80ng/ml corresponding to a Specific Activity of 12,500-125,000IU/mg.

    Citations

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 7 (CCL7) is a small cytokine known as a chemokine that was previously called monocyte-specific chemokine 3 (MCP3). Due to CCL7 possessing two adjacent N-terminal cysteine residues in its mature protein, it is classified among the subfamily of chemokines known as CC chemokines. CCL7 specifically attracts monocytes, and regulates macrophage function. It is produced by certain tumor cell lines and by macrophages. This chemokine is located on chromosome 17 in humans, in a large cluster containing many other CC chemokines and is most closely related to CCL2(previously called MCP1).

    • Synonyms

      Small inducible cytokine A7, CCL7, Monocyte chemotactic protein 3, MCP-3, Monocyte chemoattractant protein 3, NC28, chemokine (C-C motif) ligand 7, FIC, MARC, MCP3, SCYA6, SCYA7, MGC138463, MGC138465.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MCP-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL7 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 Monocyte Chemotactic Protein-3in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Gln-Pro-Val-Gly-Ile.

    • Background

      What is the molecular weight/Mw of CCL7 HUMAN Protein?
      CCL7 HUMAN Protein has a total Mw of 9.01kDa.

      What is the source or expression system of CCL7 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL7 HUMAN Protein?
      CCL7 HUMAN Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL7 HUMAN Protein?
      The specific activity as determined by the ability of MCP-3 to chemoattract human peripheral blood at 8 - 80ng/ml corresponding to a Specific Activity of 12,500-125,000IU/mg.

      What is the amino acid sequence of CCL7 HUMAN Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Gln-Pro-Val-Gly-Ile.

      What applications can CCL7 HUMAN Protein be used in?
      CCL7 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL7 HUMAN Protein?
      The endotoxin level is minimal, CCL7 HUMAN 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.

    Mcp 3 Human
  • View Data Sheet

    Name :

    CTSZ Human, Sf9

    Description:

    Cathepsin-Z Human Recombinant, Sf9

    Cathepsin Z, Cathepsin X, Cysteine-Type Carboxypeptidase, Lysosomal Carboxypeptidase B, Carboxypeptidase LB, Cathepsin B2, Cathepsin IV, Cathepsin Z1, Cathepsin P, Cathepsin Y, EC 3.4.18.1, Preprocathepsin P, CTSX.

    Product # :

    ENZ-1097

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    Description

    CTSZ produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 288 amino acids (24-303.a.) and having a molecular mass of 32.5kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).CTSZ is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    The specific activity is determent as the ability of 1 unit to convert 1.0 pmole of Mca-PLGL-Dpa-AR-NH2 to MCA- Pro-Leu-OH per minute at pH 3.5 at 25C and is > 1,400 pmol/min/ug.

    Citations

    More Info

    • Introduction

      Cathepsin-Z (CTSZ) is a lysosomal cysteine proteinase and a member of the peptidase C1 family. CTSZ, which is known also as cathepsin X and cathepsin P, exhibits carboxy-monopeptidase and carboxy-dipeptidase activities. CTSZ is expressed ubiquitously in cancer cell lines and primary tumors and as other members of this family, takes part in tumorigenesis.

    • Synonyms

      Cathepsin Z, Cathepsin X, Cysteine-Type Carboxypeptidase, Lysosomal Carboxypeptidase B, Carboxypeptidase LB, Cathepsin B2, Cathepsin IV, Cathepsin Z1, Cathepsin P, Cathepsin Y, EC 3.4.18.1, Preprocathepsin P, CTSX.

    • 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

      GLYFRRGQTC YRPLRGDGLA PLGRSTYPRP HEYLSPADLP KSWDWRNVDG VNYASITRNQ
      HIPQYCGSCW AHASTSAMAD RINIKRKGAW PSTLLSVQNV IDCGNAGSCE GGNDLSVWDY
      AHQHGIPDET CNNYQAKDQE CDKFNQCGTC NEFKECHAIR NYTLWRVGDY GSLSGREKMM
      AEIYANGPIS CGIMATERLA NYTGGIYAEY QDTTYINHVV SVAGWGISDG TEYWIVRNSW
      GEPWGERGWL RIVTSTYKDG KGARYNLAIE EHCTFGDPIV LEHHHHHH

    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.

    Cathepsin Z Protein
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