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  • Aprotinin

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Search results

1000 results found for “fibronectin”

Name

Description

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  • View Data Sheet

    Name :

    PhI p 1

    Description:

    Pollen allergen Phl p 1 Recombinant

    Pollen allergen Phl p 1, Allergen Phl p I, Phl p 1, PHLPI.

    Product # :

    PRO-2305

    Price :

    Quantity :

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    • description
    • source
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    Description

    Recombinant Pollen allergen Phl p 1 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 29,516 Dalton. PhI p 1 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    PhI p 1 protein solution is supplied in 20mM HEPES pH-8.0, 200mM NaCl and 20% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Pollen allergen Phl p 1 (PhI p 1) causes an allergic reaction in humans.

    • Synonyms

      Pollen allergen Phl p 1, Allergen Phl p I, Phl p 1, PHLPI.

    • 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. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.

    • Molar extinction coefficient

      46785; A280(1mg/ml)=1.699

    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.

    Phi P 1
  • View Data Sheet

    Name :

    LMNA Human

    Description:

    Lamin A/C Human Recombinant

    Prelamin-A/C, Lamin-A/C, 70 kDa lamin, LMNA, LMN1, Renal carcinoma antigen NY-REN-32, Progerin.

    Product # :

    PRO-2666

    Price :

    Quantity :

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    • More Info

    Description

    LMNA Human Recombinant fused with a His tag produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 614 amino acids and having a molecular mass of 68.0kDa. The LMNA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LMNA solution contains 20mM Tris-HCl pH 7.5, 1mM DTT, 0.5M NaCl, 1.5mM EDTA and 20%(v/v) glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lamin-A is a major component of the nuclear lamina, a dynamic meshwork located just under the nuclear envelope and it is encoded by lamin A/C gene (LMNA).
      Lamin-A is synthesized as Prelamin A, a longer precursor that in vivo goes through a serial post-translational modifications that lead to mature Lamin A.
      Diverse mutations in the Lamin A/C gene are associated with different diseases that are collectively called laminophaties, including Emery-Dreifuss muscular dystrophy, familiar partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease, and Hutchinson-Gilford progeria syndrome.

    • Synonyms

      Prelamin-A/C, Lamin-A/C, 70 kDa lamin, LMNA, LMN1, Renal carcinoma antigen NY-REN-32, Progerin.

    • 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

      MAHHHHHHVG TGSNDDDDKS PDMETPSQRR ATRSGAQASS TPLSPTRITR LQEKEDLQEL NDRLAVYIDR VRSLETENAG LRLRITESEE VVSREVSGI KAAYEAELGD ARKTLDSVAK ERARLQLELS KVREEFKELK ARNTKKEGDL IAAQARLKDL EALLNSKEAA LSTALSEKRT LEGELHDLRG QVAKLEAALG EAKKQLQDEM LRRVDAENRL QTMKEELDFQ KNIYSEELRE TKRRHETRLV EIDNGKQREF ESRLADALQE LRAQHEDQVE QYKKELEKTY SAKLDNARQS AERNSNLVGA AHEELQQSRI RIDSLSAQLS QLQKQLAAKE AKLRDLEDSL ARERDTSRRL LAEKEREMAE MRARMQQQLD EYQELLDIKL ALDMEIHAYR KLLEGEEERL RLSPSPTSQR SRGRASSHSS QTQGGGSVTK KRKLESTESR SSFSQHARTS GRVAVEEVDE EGKFVRLRNK SNEDQSMGNW QIKRQNGDDP LLTYRFPPKF TLKAGQVVTI WAAGAGATHS PPTDLVWKAQ NTWGCGNSLR TALINSTGEE VAMRKLVRSV TVVEDDEDED GDDLLHHHHG SHCSSSGDPA EYNLRSRTVL CGTCGQPADK ASASGSGAQS PQNCSIM

    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.

    Lmna Human
  • View Data Sheet

    Name :

    Cys-Protein-A/G/L

    Description:

    Cys-Protein A/G/L Recombinant

    Product # :

    PRO-1935

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
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    Description

    Recombinant Protein-A/G/L produced in E.Coli is a single non-glycosylated polypeptide chain fused with a Cys at N-terminus. Protein- A/G/L is comprised of 5 IgG-binding regions of Protein A (E-D-A-B-C), 2 of protein G (C1-C3) and 5 of Protein L (B1-B2-B3-B4-B5) containing 806 amino acids in total and having a molecular mass of 89.3kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein- A/G/L to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    Protein- A/G/L was lyophilized without any additives.

    Purity

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

    More Info

    • Introduction

      The recombinant Protein A/G/L is a genetically engineered protein which combines the IgG binding profiles of all Protein A, Protein G and Protein L. Protein A/G/L is a gene fusion product. Recombinant fusion protein A/G/L is comprised of 5 Ig-binding regions of protein L (B1-B2-B3-B4-B5), 5 IgG binding domains from Protein A (E-D-A-B-C) and 2 Ig-binding region of protein G (C1-C3). The recombinant Protein A/G/L is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G/L binds to IgG from humans, mice, rats, cows, goats, sheep, rabbits, guinea pigs, pigs, dogs and cats.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Protein-A/G/L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-A/G/L 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 Protein-A/G/L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      CNAAQHDEAQ QNAFYQVLNM PNLNADQRNG FIQSLKDDPS QSANVLGEAQ KLNDSQAPKA DAQQNNFNKD QQSAFYEILN MPNLNEAQRN GFIQSLKDDP SQSTNVLGEA KKLNESQAPK ADNNFNKEQQ NAFYEILNMP NLNEEQRNGF IQSLKDDPSQ SANLLSEAKK LNESQAPKAD NKFNKEQQNA FYEILHLPNL NEEQRNGFIQ SLKDDPSQSA NLLAEAKKLN DAQAPKADNK FNKEQQNAFY EILHLPNLTE EQRNGFIQSL KDDPSVSKEI LAEAKKLNDA QAPKEEDSLE GSGSGTYKLI LNGKTLKGET TTEAVDAATA EKVFKQYAND NGVDGEWTYD DATKTFTVTE KPEVIDASEL TPAVTTYKLV INGKTLKGET TTKAVDAETA EKAFKQYAND NGVDGVWTYD DATKTFTVTE EPRARPGSGS GKEETPETPE TDSEEEVTIK ANLIFANGST QTAEFKGTFE KATSEAYAYA DTLKKDNGEY TVDVADKGYT LNIKFAGKEK TPEEPKEEVT IKANLIYADG KTQTAEFKGT FEEATAEAYR YADALKKDNG EYTVDVADKG YTLNIKFAGK EKTPEEPKEE VTIKANLIYA DGKTQTAEFK GTFEEATAEA YRYADLLAKE NGKYTVDVAD KGYTLNIKFA GKEKTPEEPK EEVTIKANLI YADGKTQTAE FKGTFAEATA EAYRYADLLA KENGKYTADL EDGGYTINIR FAGKKVDEKP EEKEQVTIKE NIYFEDGTVQ TATFKGTFAE ATAEAYRYAD LLSKEHGKYT ADLEDGGYTI NIRFAG.

    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.

    Cys Protein A G L
  • View Data Sheet

    Name :

    FGF 9 Human

    Description:

    Fibroblast Growth Factor-9 Human Recombinant

    GAF (Glia-activating factor), HBGF-9, MGC119914, MGC119915, FGF-9.

    Product # :

    CYT-415

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info

    Description

    Fibroblast Growth Factor-9 Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids and having a molecular mass of 23.4 kDa. The FGF-9 is purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The sterile protein powder is lyophilized from 1mg/ml solution containing 1xPBS.

    Purity

    Greater than 95.0% as determined by RP-HPLC and SDS-PAGE.

    Biological Activity

    The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <0.5ng/ml, corresponding to a specific activity of 2,000,000 Units/mg.

    More Info

    • Introduction

      The human FGF-9 cDNA encodes a 208 amino acid residue protein that contains a single, potential N-linked glycosylation site. The native protein is glycosylated and is efficiently secreted after synthesis, although FGF -9 lacks a typical secretion signal. Rat and mouse FGF-9 show a very high homology to human FGF-9. The transcripts for FGF-9 have been found in brain and in kidney tissue. Fibroblast Growth Factor-9 is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF9 was isolated as a secreted factor that exhibits a growth-stimulating effect on cultured glial cells. In nervous system, this protein is produced mainly by neurons and may be important for glial cell development. Expression of the mouse homolog of this gene was found to be dependent on Sonic hedgehog (Shh) signaling. Mice lacking the homolog gene displayed a male-to-female sex reversal phenotype, which suggested a role in testicular embryogenesis Fibroblast Growth Factor 9 may have a role in glial cell growth and differentiation during development, gliosis during repair and regeneration of brain tissue after damage, differentiation and survival of neuronal cells, and growth stimulation of glial tumors.

    • Synonyms

      GAF (Glia-activating factor), HBGF-9, MGC119914, MGC119915, FGF-9.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Lyophilized Fibroblast Growth Factor 9 Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-9 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 Fibroblast Growth Factor-9 Human Recombinant sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APLGEVGNYF GVQDAVPFGN VPVLPVDSPV LLSDHLGQSE AGGLPRGPAV
      TDLDHLKGIL RRRQLYCRTG FHLEIFPNGT IQGTRKDHSR FGILEFISIA
      VGLVSIRGVD SGLYLGMNEK GELYGSEKLT QECVFREQFE ENWYNTYSSN
      LYKHVDTGRR YYVALNKDGT PREGTRTKRH QKFTHFLPRP VDPDKVPELY
      KDILSQS.

    • Background

      What is the molecular weight/Mw of FGF9 Protein?
      FGF9 Protein has a total Mw of 23.4kDa.

      What is the source or expression system of FGF9 Protein?
      Escherichia Coli.

      What is the Purity of FGF9 Protein?
      FGF9 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF9 Protein?
      The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <0.5ng/ml, corresponding to a specific activity of 2,000,000 Units/mg.

      What is the amino acid sequence of FGF9 Protein?
      APLGEVGNYF GVQDAVPFGN VPVLPVDSPV LLSDHLGQSE AGGLPRGPAV
      TDLDHLKGIL RRRQLYCRTG FHLEIFPNGT IQGTRKDHSR FGILEFISIA
      VGLVSIRGVD SGLYLGMNEK GELYGSEKLT QECVFREQFE ENWYNTYSSN
      LYKHVDTGRR YYVALNKDGT PREGTRTKRH QKFTHFLPRP VDPDKVPELY
      KDILSQS.

      What applications can FGF9 Protein be used in?
      FGF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF9 Protein?
      The endotoxin level is minimal, FGF9 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.

    Fgf9 Human
  • View Data Sheet

    Name :

    LECT1 Human

    Description:

    Leukocyte Cell Derived Chemotaxin 1 Human Recombinant

    BRICD3, CHM-I, CHM1, MYETS1, Leukocyte cell-derived chemotaxin 1, Chondrosurfactant protein, CH-SP, Chondromodulin-1, ChM-I, LECT1.

    Product # :

    PRO-1846

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    Description

    LECT1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 144 amino acids (214-334) and having a molecular mass of 16.3kDa. LECT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LECT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Leukocyte Cell Derived Chemotaxin 1, also known as LECT1, is a glycosylated transmembrane protein which is cleaved to form a mature, secreted protein. The mature protein encourages chondrocyte growth and inhibits angiogenesis. The mature protein takes part in endochondral bone development by permitting cartilaginous anlagen to be vascularized and replaced by bone. LECT1 is expressed in the avascular area of prehypertrophic cartilage and its expression reduces during vascular invasion and chondrocyte hypertrophy.

    • Synonyms

      BRICD3, CHM-I, CHM1, MYETS1, Leukocyte cell-derived chemotaxin 1, Chondrosurfactant protein, CH-SP, Chondromodulin-1, ChM-I, LECT1.

    • 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 MGSREVVRKI VPTTTKRPHS GPRSNPGAGR LNNETRPSVQ EDSQAFNPDN PYHQQEGESM TFDPRLDHEG ICCIECRRSY THCQKICEPL GGYYPWPYNY QGCRSACRVI MPCSWWVARI LGMV.

    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.

    Lect1 Human
  • View Data Sheet

    Name :

    C4c Human

    Description:

    Complement Component C4c Human

    Complement C4c, Complement Component C4c, C4c.

    Product # :

    PRO-556

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    Description

    Human C4c produced in Human plasma having a molecular mass of 210 kDa.

    Source

    Human Plasma.

    Formulation

    The Human Complement C4c solution is in Sodium Phosphate buffer pH 7.0 containing 0.15M NaCl and 0.09% NaN3.

    Purity

    Greater than 99.0%.

    More Info

    • Introduction

      Complement C4c is a degradation product of C4b which is cleaved by C4b/C3b inactivator to yield C4d and C4c.
      Complement C4c interacts with C1 and C2 to form C3 convertase of the classic activation pathway. Systemic lupus erythematosus (SLE) is often associated with congenital C4 deficiency. Reduced levels of components of the classic pathway (C1, C2, C4, C3) are common after such activation, e.g. in SLE, acute serum sickness and conditions associated with circulating immune complexes.

    • Synonyms

      Complement C4c, Complement Component C4c, C4c.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Human C4c although stable at 4°C for 1 week, should be stored at -15°C.Please avoid freeze-thaw cycles.

    • Human Virus Test

      Plasma from each donor has been tested and found negative for HIV-1 & 2 antibodies, Hepatatis B surface antigen, and Hepatatis C antibodies.

    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.

    Complement C4C Human
  • View Data Sheet

    Name :

    AGO2 Human

    Description:

    Argonaute 2 Human Recombinant

    Protein argonaute-2, Argonaute2, hAgo2, Argonaute RISC catalytic component 2, Eukaryotic translation initiation factor 2C 2, eIF-2C 2, eIF2C 2, PAZ Piwi domain protein, PPD, AGO2, EIF2C2, Protein slicer.

    Product # :

    PRO-2577

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    Description

    AGO2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 1-859) containing 869 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 98.4kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    AGO2 filltered solution in 50mM acetate buffer, pH 4.0 and 20% (w/v) glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The Argonaute protein is part of the RISC or RNA-induced silencing complex, as so, the protein has a key part in the slicing processes of RNA. The RNA interference (RNAi) is being held by RISC. Small non-coding RNA fragments bond to the Argonaute proteins, through base pairing, eventually leads to the cleavage of messenger RNA or translation suppression.

    • Synonyms

      Protein argonaute-2, Argonaute2, hAgo2, Argonaute RISC catalytic component 2, Eukaryotic translation initiation factor 2C 2, eIF-2C 2, eIF2C 2, PAZ Piwi domain protein, PPD, AGO2, EIF2C2, Protein slicer.

    • Physical Appearance

      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

      MKHHHHHHAS MYSGAGPALA PPAPPPPIQG YAFKPPPRPD FGTSGRTIKL QANFFEMDIP KIDIYHYELD IKPEKCPRRV NREIVEHMVQ HFKTQIFGDR KPVFDGRKNL YTAMPLPIGR DKVELEVTLP GEGKDRIFKV SIKWVSCVSL QALHDALSGR LPSVPFETIQ ALDVVMRHLP SMRYTPVGRS FFTASEGCSN PLGGGREVWF GFHQSVRPSL WKMMLNIDVS ATAFYKAQPV IEFVCEVLDF KSIEEQQKPL TDSQRVKFTK EIKGLKVEIT HCGQMKRKYR VCNVTRRPAS HQTFPLQQES GQTVECTVAQ YFKDRHKLVL RYPHLPCLQV GQEQKHTYLP LEVCNIVAGQ RCIKKLTDNQ TSTMIRATAR SAPDRQEEIS KLMRSASFNT DPYVREFGIM VKDEMTDVTG RVLQPPSILY GGRNKAIATP VQGVWDMRNK QFHTGIEIKV WAIACFAPQR QCTEVHLKSF TEQLRKISRD AGMPIQGQPC FCKYAQGADS VEPMFRHLKN TYAGLQLVVV ILPGKTPVYA EVKRVGDTVL GMATQCVQMK NVQRTTPQTL SNLCLKINVK LGGVNNILLP QGRPPVFQQP VIFLGADVTH PPAGDGKKPS IAAVVGSMDA HPNRYCATVR VQQHRQEIIQ DLAAMVRELL IQFYKSTRFK PTRIIFYRDG VSEGQFQQVL HHELLAIREA CIKLEKDYQP GITFIVVQKR HHTRLFCTDK NERVGKSGNI PAGTTVDTKI THPTEFDFYL CSHAGIQGTS RPSHYHVLWD DNRFSSDELQ ILTYQLCHTY VRCTRSVSIP APAYYAHLVA FRARYHLVDK EHDSAEGSHT SGQSNGRDHQ ALAKAVQVHQ DTLRTMYFA.

    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.

    Ago2 Human
  • View Data Sheet

    Name :

    CLEC7A Human

    Description:

    C-Type Lectin Domain Family 7, Member A Human Recombinant

    BGR, Dendritic Cell-Associated C-Type Lectin-1, Dendritic Cell-Associated C-Type Lectin 1, C-Type Lectin Domain Family 7, Member A, Lectin-Like Receptor 1, CD369 Antigen, CANDF4, SCARE2, CD369, C-Type Lectin Domain Containing 7A, C-Type Lectin Domain Family 7 Member A, C-Type (Calcium Dependent, Carbohydrate-Recognition Domain) Lectin, Superfamily Member 12, C-Type Lectin Superfamily Member 12, DC-Associated C-Type Lectin 1, Beta-Glucan Receptor, Dectin-1, CLECSF12, DECTIN1.

    Product # :

    PRO-2634

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    Description

    CLEC7A Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 183 amino acids (71-244 a.a) and having a molecular mass of 21kDa. CLEC7A is fused to a 9 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The CLEC7A solution (0.5mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      C-type lectin domain family 7 member A 1 or CLEC7A is a protein, that in the innate immune system, acts against fungal pathogens. CLEC7A can be found in the immune system response cells such as monocytes, macrophages & neutrophils, or in dendritic and T cells. The protein is enhanced by macrophages by using GM-CSF, IL-4, or IL-13, or diminishes by dexamethasone, IL-10 and LPS.

    • Synonyms

      BGR, Dendritic Cell-Associated C-Type Lectin-1, Dendritic Cell-Associated C-Type Lectin 1, C-Type Lectin Domain Family 7, Member A, Lectin-Like Receptor 1, CD369 Antigen, CANDF4, SCARE2, CD369, C-Type Lectin Domain Containing 7A, C-Type Lectin Domain Family 7 Member A, C-Type (Calcium Dependent, Carbohydrate-Recognition Domain) Lectin, Superfamily Member 12, C-Type Lectin Superfamily Member 12, DC-Associated C-Type Lectin 1, Beta-Glucan Receptor, Dectin-1, CLECSF12, DECTIN1.

    • 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

      ADPRHNSGRN PEEKDNFLSR NKENHKPTES SLDEKVAPSK ASQTTGGFSQ SCLPNWIMHG KSCYLFSFSG NSWYGSKRHC SQLGAHLLKI DNSKEFEFIE SQTSSHRINA FWIGLSRNQS EGPWFWEDGS AFFPNSFQVR NTVPQESLLH NCVWIHGSEV YNQICNTSSY SICEKELHHH HHH.

    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.

    Clec7A Human
  • View Data Sheet

    Name :

    OPG Human

    Description:

    Osteoprotegerin Human Recombinant

    TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, Osteoprotegerin, TR1, MGC29565.

    Product # :

    CYT-177

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    Description

    Recombinant Human Osteoprotegerin produced in E.coli cells is a single, non-glycosylated, polypeptide chain containing 174 amino acids and having a molecular mass of 20kDa. The OPG is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The OPG was lyophilized from a 0.2µm filtered concentrated (0.5mg/ml) solution in PBS, pH 7.4.

    Purity

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

    Biological Activity

    The activity is determined by its ability to neutralize the stimulation of U937 cells treated with 10ng/ml of soluble RANKL corresponding to a specific activity of 100,000IU/mg.

    More Info

    • Introduction

      Osteoprotegerin acts as decoy receptor for rankl and thereby neutralizes its function in osteoclastogenesis. OPG inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local rankl/opg ratio. Osteoprotegerin may also play a role in preventing arterial calcification. May act as decoy receptor for trail and protect against apoptosis. Trail binding blocks the inhibition of osteoclastogenesis.

    • Synonyms

      TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, Osteoprotegerin, TR1, MGC29565.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      METFPPKYLH YDEETSHQLL CDKCPPGTYL KQHCTAKWKT VCAPCPDHYY TDSWHTSDEC LYCSPVCKEL QYVKQECNRT HNRVCECKEG RYLEIEFCLK HRSCPPGFGV VQAGTPERNT VCKRCPDGFF SNETSSKAPC RKHTNCSVFG LLLTQKGNAT HDNICSGNSE STQK.

    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.

    Opg Human
  • View Data Sheet

    Name :

    Periostin Human

    Description:

    Periostin Human Recombinant

    OSF-2, Periostin, Osteoblast Specific Factor 2, PN OSF-2, PDLPOSTN, POSTN, MGC119510, MGC119511, PN, RP11-412K4.1.

    Product # :

    CYT-452

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    Description

    The OSF2 His-Tagged Fusion Protein Human is produced in E. coli, and its molecular weight is 75 kDa protein containing 648 amino acid residues of the human OSF-2 and 23 additional amino acid residues - HisTag, Xa - cleavage site.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4 µm) and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Periostin is a disulfide linked 90 kDa, 811 amino acid protein originally isolated as a osteoblast-specific factor that functions as a cell adhesion molecule for preosteoblasts and is thought to be involved in osteoblast recruitment, attachment and spreading. Additionally, periostin expression has previously been shown to be significantly increased by both transforming growth factor beta-1(TGFbeta1) and bone morphogenetic protein (BMP-2). OSF-2 has a typical signal sequence, followed by a cysteine-rich domain, a fourfold repeated domain and a C-terminal domain. The fourfold repeated domain of OSF-2 shows homology with the insect protein fasciclin
      Periostin mRNA is expressed in the developing mouse embryonic and fetal heart, and that it is localized to the endocardial cushions that ultimately divide the primitive heart tube into a four-chambered heart.

    • Synonyms

      OSF-2, Periostin, Osteoblast Specific Factor 2, PN OSF-2, PDLPOSTN, POSTN, MGC119510, MGC119511, PN, RP11-412K4.1.

    • 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 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MGHHHHHHHH HHSSGHIEGR HMRNNHYDKI LAHSRIRGRD QGPNVCALQQ ILGTKKKYFS TCKNWYKKSI CGQKTTVLYE CCPGYMRMEG MKGCPAVLPI DHVYGTLGIV GATTTQRYSD ASKLREEIEG KGSFTYFAPS NEAWDNLDSD IRRGLESNVN VELLNALHSH MINKRMLTKD LKNGMIIPSM YNNLGLFINH YPNGVVTVNC ARIIHGNQIA TNGVVHVIDR VLTQIGTSIQ DFIEAEDDLS SFRAAAITSD ILEALGRDGH FTLFAPTNEA FEKLPRGVLE RFMGDKVASEALMKYHILNT LQCSESIMGG AVFETLEGNT IEIGCDGDSI TVNGIKMVNK KDIVTNNGVI HLIDQVLIPD SAKQVIELAG KQQTTFTDLV AQLGLASALR PDGEYTLLAP VNNAFSDDTL SMVQRLLKLI LQNHILKVKV GLNELYNGQI LETIGGKQLR VFVYRTAVCI ENSCMEKGSK QGRNGAIHIF REIIKPAEKS LHEKLKQDKR FSTFLSLLEA ADLKELLTQP GDWTLFVPTN DAFKGMTSEE KEILIRDKNA LQNIILYHLT PGVFIGKGFE PGVTNILKTT QGSKIFLKEV NDTLLVNELK SKESDIMTTN GVIHVVDKLL YPADTPVGND QLLEILNKLI KYIQIKFVRG STFKEIPVTV Y.

    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.

    Periostin Human
  • View Data Sheet

    Name :

    Follistatin Human, His

    Description:

    Follistatin Human Recombinant, His Tag

    FST, FS, Activin-binding protein.

    Product # :

    CYT-029

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    Description

    FST His Protein is 36.0 kDa protein containing 325 amino acid residues of the FST His and the 10 aa N-Terminal His-tag.

    Source

    E. coli.

    Formulation

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

    More Info

    • Introduction

      Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release. The single FST gene encodes two isoforms, FST317 and FST344 containing 317 and 344 amino acids respectively, resulting from alternative splicing of the precursor mRNA. In a study in which 37 candidate genes were tested for linkage and association with polycystic ovary syndrome (PCOS) or hyperandrogenemia in 150 families, evidence was found for linkage between PCOS and follistatin. Follistatin binds directly to activin and functions as an activin antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).

    • Synonyms

      FST, FS, Activin-binding protein.

    • Stability

      Store lyophilized FST His at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted FST His 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. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS GNCWLRQAKN GRCQVLYKTE LSKEECCSTG RLSTSWTEED VNDNTLFKWM IFNGGAPNCI PCKETCENVD CGPGKKCRMN KKNKPRCVCA PDCSNITWKG PVCGLDGKTY RNECALLKAR CKEQPELEVQ YQGRCKKTCR DVFCPGSSTC VVDQTNNAYC VTCNRICPEP ASSEQYLCGN DGVTYSSACH LRKATCLLGR SIGLAYEGKC IKAKSCEDIQ CTGGKKCLWD FKVGRGRCSL CDELCPDSKS DEPVCASDNA TYASECAMKE AACSSGVLLE VKHSGSCNSI SEDTEEEEED EDQDYSFPIS SILEW.

    • Background

      What is the molecular weight/Mw of FOLLISTATIN HUMAN, HIS Protein?
      FOLLISTATIN HUMAN, HIS Protein has a total Mw of 36kDa.

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

      What is the Biological Activity of FOLLISTATIN HUMAN, HIS Protein?
      The biological functionality of FOLLISTATIN HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of FOLLISTATIN HUMAN, HIS Protein?
      MKHHHHHHAS GNCWLRQAKN GRCQVLYKTE LSKEECCSTG RLSTSWTEED VNDNTLFKWM IFNGGAPNCI PCKETCENVD CGPGKKCRMN KKNKPRCVCA PDCSNITWKG PVCGLDGKTY RNECALLKAR CKEQPELEVQ YQGRCKKTCR DVFCPGSSTC VVDQTNNAYC VTCNRICPEP ASSEQYLCGN DGVTYSSACH LRKATCLLGR SIGLAYEGKC IKAKSCEDIQ CTGGKKCLWD FKVGRGRCSL CDELCPDSKS DEPVCASDNA TYASECAMKE AACSSGVLLE VKHSGSCNSI SEDTEEEEED EDQDYSFPIS SILEW.

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

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

    Fst His Human
  • View Data Sheet

    Name :

    FHIT Human, GST

    Description:

    Fragile Histidine Triad Human Recombinant, GST Tag

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

    Product # :

    PRO-297

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    Description

    FHIT Human Recombinant full length protein expressed in E.coli, shows a 43 kDa band on SDS-PAGE. The FHIT is fused to GST-Tag and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FHIT in 50mM Tris-Acetate, pH7.5, 1mM EDTA and 20% Glycerol.

    More Info

    • Introduction

      FHIT is a member of the histidine triad gene family. FHIT gene encodes a diadenosine 5',5'''-P1,P3-triphosphate hydrolase involved in purine metabolism. FHIT gene includes the common fragile site FRA3B on chromosome 3, where carcinogen-induced damage can lead to translocations and abnormal transcripts of this gene. The FHIT protein is a tumor suppressor with reduced or no expression in numerous types of cancer. FHIT may also act as a tumor suppressor in normal cells. Alterations and deletions of the FHIT (Fragile Histidine Triad) gene are strongly linked to the genesis and establishment of human tumors of the lung, cervix, breast, colon, stomach, and pancreas. The expression of FHIT is more often lost in cancers of individuals with familial mutations causing deficiency in DNA repair genes such as BRCA1, BRCA2 and MSH2. In vitro FHIT functions as a hydrolase that cleaves diadenosine triphosphate (Ap3A) to ADP and AMP. The FHIT -Ap3A enzyme-substrate complex seems to be the tumor suppressor signal. The restoration of FHIT expression in FHIT -deficient cancer cells leads to apoptosis, involving the intrinsic caspase pathway, in cancer-derived cells and in tumor xenografts.

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months.Please prevent freeze-thaw cycles.

    • Applications

      • ELISA
      • Inhibition Assays
      • Western Blotting.

    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 Gst
  • View Data Sheet

    Name :

    Gliadin Gamma Wheat

    Description:

    Gliadin Gamma Wheat Recombinant

    Product # :

    PRO-2148

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    Description

    Recombinant Wheat Gliadin Gamma protein produced in E.Coli and fused to a 6 His Tag at C-terminus, having a theoretical Mw of 37945.14 Dalton, pI 7.70.Purified by proprietary chromatographic technique.

    Source

    Escherichia Coli.

    Formulation

    Gliadin Gamma protein solution (1mg/ml) in 10mM Tris-HCl pH 7.2.

    Purity

    Protein is >90% pure.

    More Info

    • Introduction

      Wheat Gliadin and related gluten components from barley, rye and possibly oats can cause an abnormal immune response called Celiac disease which is a chronic gastrointestinal disorder. Celiac disease characteristics are flattening of the jejunal mucosa and intestinal lesions of variable severity in hereditarily inclined individuals. Even though Celiac disease is not a classic autoimmune disease it is related to anti-tissue transglutaminase antibodies and gliadin antibodies tests are most recommended in screening populations at risk for CD and other gluten-sensitive enteropathies. In the past, serologic tests for gliadin antibodies usually were not very precise and were not enough for accurate diagnosis due to missing deamidated epitopes within the authentic gliadin fraction traditionally used in diagnostic test kits. ProSpec's deamidated Gliadin isoform matches to the deamidated neo-epitopes, which in the natural antigen are formed by transglutaminase-mediated glutamine side chain deamidation.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Gliadin Gamma although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MKTLLILTILAMAITIGTANIQVDPSGQVQWLQQQLVPQLQQPLSQQPQQTFPQPQQTFPH
      QPQQQVPQPQQPQQPFLQPQQPFPQQPQQPFPQTQQPQQPFPQQPQQPFPQTQQPQQ
      PFPQQPQQPFPQTQQPQQPFPQLQQPQQPFPQPQQQLPQPQQPQQSFPQQQRPFIQPSL
      QQQLNCKNILLQQSKPASLVSSLWSIIWPQSDCQVMRQQCCQQLAQIPQQLQCAAIHSVVH
      SIIMQQQQQQQQQQGIDIFLPLSQHEQVGQGSLVQGQGIIQPQQPAQLEAIRSLVLQTLPSM
      CNVYVPPECSIMRAPFASIVAGIGGQHHHHHH.

    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.

    Gliadin Gamma Wheat
  • View Data Sheet

    Name :

    Leptin Human, PEG

    Description:

    Leptin Human Recombinant, PEG

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-1108

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    Description

    Pegylated Leptin Human Recombinant produced in E.Coli is a single non-glycosilated polypeptide chain containing 146 amino acids, an additional Ala at N-terminus and one molecule of PEG 20 kDa at its N-terminus acids and having a molecular weight of 35.6kDa. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 100 kDa protein. Pegylated Leptin Human Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

    Purity

    Greater than 98.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Biological Activity is < than 0.1% as determined by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It’s in vitro activity is 5-7 fold lower than the non-pegylated recombinant human leptin but in vivo it has profound weight reducing effect, resulting mainly from reduced food intake.

    More Info

    • Introduction

      Leptin takes an important part in the regulation of energy balance and body weight control.After entering the circulation, Leptin binds LEPRwhich results in the activation of several major signalling pathways. In the hypothalamus Leptin acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption and also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, regulates pancreatic beta-cell function and insulin secretion and affects innate and adaptive immunity.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Pegylated leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution leptin N82K 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 Pegylated leptin in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.87 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

    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.

    Leptin Mutant
  • View Data Sheet

    Name :

    EPO, Clone PAT1C12AT

    Description:

    Erythropoietin clone PAT1C12AT, Mouse Anti Human

    EPO-a, EPO-alpha, Epoetin, EP, MGC138142.

    Product # :

    ANT-744

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    Formulation

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

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    • Introduction

      EPO is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of 4 alpha helical bundles. EPO is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. EPO also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.

    • Synonyms

      EPO-a, EPO-alpha, Epoetin, EP, MGC138142.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      PAT1C12AT.

    • Type

      Mouse Anti Human Monoclonal.

    • Purification Method

      EPO 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.

    Epo Antibody
  • View Data Sheet

    Name :

    SPP1 Human, Active

    Description:

    Osteopontin Human Recombinant, BioActive

    OPN, SPP-1, BNSP, BSPI, ETA-1, Bone sialoprotein 1, BSP I.Early T lymphocyte activation 1, ETA 1, ETA1, MGC110940, Nephropontin, Secreted phosphoprotein 1, SPP 1, SPP1, urinary stone protein, uropontin.

    Product # :

    CYT-1166

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    Description

    SPP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 321 amino acids (17-314 a.a.) and having a molecular mass of 36.2kDa. SPP1 is fused to a 23 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SPP1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 1mM DTT, 10% glycerol and 2mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by the ability of the immobilized protein to support the adhesion of HEK293 human embryonic kidney cells. When cells are added to OPN coated plates 10ug/ml. This effect is more to 40%.

    More Info

    • Introduction

      Osteopontin is a glycoprotein that was primarilyfound in osteoblasts and takes part in bone remodeling, immune functions in fibroblasts, macrophages, & lymphocytes during inflammation and wound healing. SPP1 highlybinds to hydroxyapatite. SPP1 forms an integral part of the mineralized matrix. SPP1 is vital to cell-matrix interaction.
      Secreted Phosphoprotein-1 protects against cardiac ischemia-reperfusion injury through late preconditioning. Expression of Ostepontin and CD44 in hepatocellular carcinoma is linked to advanced tumor stage &leads to prognosis information. SPP1 is the most over-expressed gene in intrahepatic cholangiocarcinoma. Secreted Phosphoprotein-1 overexpression is related with interstitial lung diseases.

    • Synonyms

      OPN, SPP-1, BNSP, BSPI, ETA-1, Bone sialoprotein 1, BSP I.Early T lymphocyte activation 1, ETA 1, ETA1, MGC110940, Nephropontin, Secreted phosphoprotein 1, SPP 1, SPP1, urinary stone protein, uropontin.

    • Physical Appearance

      Sterile Filtered clear 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 RSMIPVKQAD SGSSEEKQLY NKYPDAVATW LNPDPSQKQN LLAPQNAVSS EETNDFKQET LPSKSNESHD HMDDMDDEDD DDHVDSQDSI DSNDSDDVDD TDDSHQSDES HHSDESDELV TDFPTDLPAT EVFTPVVPTV DTYDGRGDSV VYGLRSKSKK FRRPDIQYPD ATDEDITSHM ESEELNGAYK AIPVAQDLNA PSDWDSRGKD SYETSQLDDQ SAETHSHKQS RLYKRKANDE SNEHSDVIDS QELSKVSREF HSHEFHSHED MLVVDPKSKE EDKHLKFRIS HELDSASSEV N.

    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.

    Osteopontin Human
  • View Data Sheet

    Name :

    Resistin Human, Antagonist

    Description:

    Resistin Antagonist Human Recombinant

    Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    Product # :

    CYT-1255

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    • More Info

    Description

    Resistin Human antagonist is a monomeric C7A mutant that does not form covalent dimers. Resistin Human antagonist is purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    Resistin was lyophilized from a concentrated (1mg/ml) solution with 0.03% NaHCO3.

    Purity

    Greater than 98.0% as determined by:

    (a) Analysis by Gel Filtration.

    (b) Analysis by SDS-PAGE.

    (c) Analysis by RP-HPLC.

    Biological Activity

    The biological activity was evidenced by resistin antagonist activity to inhibit resistin-induced Akt phosphorylation in two cell lines. It also reduced the weight (mainly the visceral fat) and normalized GTT and ITT inHFD-fed mice.

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    • Synonyms

      Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Resistin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Resistin Mouse 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 Resistin in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first seven N-terminal amino acids was determined and was found to be Ala-Ser-Ser-Lys-Thr-Leu-Ala.

    • Background

      Resistin, also known as adipose tissue-specific secretory factor (ADSF) is a cysteine-rich peptide derived from adipose tissue. Resistin takes part in the inflammatory response, glucose metabolism, and angiogenesis. Resistin blocks insulin stimulated uptake of glucose by adipocytes and promote glucose release by hepatocytes. As such,Resistin considered to participate in diet‑induced insulin-sensitivity. Resistin causes high levels of low-density lipoprotein (LDL), increasing the risk of heart disease.

    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.

    Resistin Antagonist
  • View Data Sheet

    Name :

    AFAP1 Human

    Description:

    Actin Filament Associated Protein 1 Human Recombinant

    Actin filament-associated protein 1, 110 kDa actin filament-associated protein, AFAP-110, AFAP1, AFAP, Actin Filament Associated Protein 1.

    Product # :

    PRO-1972

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    Description

    AFAP1 Human Recombinant produced in E. coli is a single polypeptide chain containing 360 amino acids (250-588) and having a molecular mass of 39.2 kDa.AFAP1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The AFAP1 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      Actin Filament Associated Protein 1 (AFAP1) is a Src binding partner. AFAP1 is a possible modulator of actin filament integrity in response to cellular signals, and is also playing a role as an adaptor protein by connecting Src family members to actin filaments. AFAP1 takes partin the development and progression of prostate adenocarcinoma by regulating cell-matrix adhesions and migration in the cancer cells.

    • Synonyms

      Actin filament-associated protein 1, 110 kDa actin filament-associated protein, AFAP-110, AFAP1, AFAP, Actin Filament Associated Protein 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 MGCSGPVDSE CPPPPSSPVH KAELEKKLSS ERPSSDGEGV VENGITTCNG KEQVKRKKSS KSEAKGTVSK VTGKKITKII SLGKKKPSTD EQTSSAEEDV PTCGYLNVLS NSRWRERWCR VKDNKLIFHK DRTDLKTHIV SIPLRGCEVI PGLDCKHPLT FRLLRNGQEV AVLEASSSED MGRWIGILLA ETGSSTDPEA LHYDYIDVEM SASVIQTAKQ TFCFMNRRVI SANPYLGGTS NGYAHPSGTA LHYDDVPCIN GSLRGKKPPV ASNGVTGKGK TLSSQPKKAD PAAVVKRTGS NAAQYKYGKN RVEADAKRLQ TKEEELLKRK EALRNRLAQL.

    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.

    Afap1 Human
  • View Data Sheet

    Name :

    SERPINA8 Human

    Description:

    Serpin Peptidase Inhibitor, Clade A Member 8 Human Recombinant

    Angiotensinogen, Serpin A8, AGT, SERPINA8, ANHU.

    Product # :

    PRO-1572

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    Description

    SERPINA8 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (a.a 34-485) containing a total of 462 amino acids, having a molecular mass of 51.0kDa (calculated) and fused to a 2 a.a C-terminal linker and an 8 a.a Flag tag at C-Terminus.The Human SERPINA8 is purified by proprietary chromatographic techniques.

    Source

    HEK 293.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Serpin Peptidase Inhibitor, Clade A Member 8 (SERPINA8), which is a pre-angiotensinogen or angiotensinogen precursor, is expressed in the liver and cleaved by the enzyme renin in response to lowered blood pressure. The ensuing product, angiotensin I, is at that point cleaved by angiotensin converting enzyme (ACE) to produce the physiologically active enzyme angiotensin II. SERPINA8 protein is involved in maintaining blood pressure and in the pathogenesis of essential hypertension and preeclampsia. SERPINA8 gene mutations are linked with susceptibility to essential hypertension, and may cause renal tubular dysgenesis, which is a severe disorder of renal tubular development. Defects in the SERPINA8 gene are also linked with non-familial structural atrial fibrillation, and inflammatory bowel disease.

    • Synonyms

      Angiotensinogen, Serpin A8, AGT, SERPINA8, ANHU.

    • 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 a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. SERPINA8 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      DRVYIHPFHL VIHNESTCEQ LAKANAGKPK DPTFIPAPIQ AKTSPVDEKA LQDQLVLVAA KLDTEDKLRA AMVGMLANFL GFRIYGMHSE LWGVVHGATV LSPTAVFGTL ASLYLGALDH TADRLQAILG VPWKDKNCTS RLDAHKVLSA LQAVQGLLVA QGRADSQAQL LLSTVVGVFT APGLHLKQPF VQGLALYTPV VLPRSLDFTE LDVAAEKIDR FMQAVTGWKT GCSLTGASVD STLAFNTYVH FQGKMKGFSL LAEPQEFWVD NSTSVSVPML SGMGTFQHWS DIQDNFSVTQ VSFTESACLL LIQPHYASDL DKVEGLTFQQ NSLNWMKKLS PRTIHLTMPQ LVLQGSYDLQ DLLAQAELPA ILHTELNLQK LSNDRIRVGE VLNSIFFELE ADEREPTEST QQLNKPEVLE VTLNRPFLFA VYDQSATALH FLGRVANPLS TART DYKDDD DK.

    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.

    Serpina8 Human
  • View Data Sheet

    Name :

    SPECC1 Human

    Description:

    Sperm Antigen With Calponin Homology And Coiled-Coil 1 Human Recombinant

    CYTSB, HCMOGT-1, HCMOGT1, NSP, Cytospin-B, Nuclear structure protein 5, NSP5, Sperm antigen HCMOGT-1, Sperm antigen with calponin homology and coiled-coil domains 1, SPECC1.

    Product # :

    PRO-2002

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    Description

    SPECC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 327 amino acids (458-761a.a) and having a molecular mass of 37.7kDa. SPECC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SPECC1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol 1mM DTT and 0.1M NaCl.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sperm Antigen With Calponin Homology And Coiled-Coil 1 (SPECC1) which is a part of the cytospin-A family takes part in cytokinesis and spindle organization. SPECC1 takes part in actin cytoskeleton organization and microtubule stabilization and therefore necessary for proper cell adhesion and migration.

    • Synonyms

      CYTSB, HCMOGT-1, HCMOGT1, NSP, Cytospin-B, Nuclear structure protein 5, NSP5, Sperm antigen HCMOGT-1, Sperm antigen with calponin homology and coiled-coil domains 1, SPECC1.

    • 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 MGSTQEGKII ELEQKCTGIL EQGRFEREKL LNIQQQLTCS LRKVEEENQG ALEMIKRLKE ENEKLNEFLE LERHNNNMMA KTLEECRVTL EGLKMENGSL KSHLQGEKQK ATEASAVEQT AESCEVQEML KVARAEKDLL ELSCNELRQE LLKANGEIKH VSSLLAKVEK DYSYLKEICD HQAEQLSRTS LKLQEKASES DAEIKDMKET IFELEDQVEQ HRAVKLHNNQ LISELESSVI KLEEQKSDLE RQLKTLTKQM KEETEEWRRF QADLQTAVVV ANDIKCEAQQ ELRTVKRKLL EEEEKNA.

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    Specc1 Human
  • View Data Sheet

    Name :

    NTS Human, sf9

    Description:

    Neurotensin Human Recombinant, sf9

    Neurotensin/neuromedin N, NTS, Neuromedin N, NN, NmN, NT, NmN-125.

    Product # :

    PRO-2374

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    • More Info

    Description

    NTS Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 134 amino acids (24-148) and having a molecular mass of 15.4kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa).NTS is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    NTS protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

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

    More Info

    • Introduction

      Neurotensin (NTS) is a common precursor for 2 peptides, neuromedin N and neurotensin. Neurotensin is a secreted tridecapeptide, which is generally distributed throughout the central nervous system, and may serve as a neurotransmitter or a neuromodulator. NTS is involved in dopamine-associated pathophysiological events, in the maintenance of gut structure and function, and in the regulation of fat metabolism. Tissue-specific processing may initiate the formation in some tissues of larger forms of neuromedin N and neurotensin. The large forms may embody more stable peptides which are also biologically active.

    • Synonyms

      Neurotensin/neuromedin N, NTS, Neuromedin N, NN, NmN, NT, NmN-125.

    • 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

      ADPSDSEEEM KALEADFLTN MHTSKISKAH VPSWKMTLLN VCSLVNNLNS PAEETGEVHE EELVARRKLP TALDGFSLEA MLTIYQLHKI CHSRAFQHWE LIQEDILDTG NDKNGKEEVI KRKIPYILHH HHHH.

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    Nts Human Sf9
  • View Data Sheet

    Name :

    OCM Human

    Description:

    Oncomodulin-1 Human Recombinant

    Oncomodulin-1, OM, Parvalbumin beta, OCM, OCM1, OCMN.

    Product # :

    PRO-143

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    • description
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    • More Info

    Description

    The Recombinant Human Oncomodulin-1 produced in E.coli has a molecular mass of 13.21kDa containing 117 amino acid residues of the human Oncomodulin-1 and fused to a 9 a.a. His tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    Oncomodulin-1 was filtered (0.4 µm) and lyophilized from 0.5 mg/ml in 20mM Tris and 50mM NaCl, pH 7.5.

    More Info

    • Introduction

      Oncomodulin is a member of the superfamily of calmodulin proteins, otherwise known as the EF-hand proteins. It is a high-affinity calcium ion-binding protein. Oncomodulin is an oncodevelopmental protein which is found in early embryonic cells in the placenta and also in tumors.

    • Synonyms

      Oncomodulin-1, OM, Parvalbumin beta, OCM, OCM1, OCMN.

    • 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 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS ITDVLSADDI S ITDVLSADDI AAALQECRDP DTFEPQKFFQ TSGLSKMSAN QVKDVFRFID NDQSGYLDEE ELKFFLQKFE SGARELTESE TKSLMAAADN DGDGKIGAEE FQEMVHS.

    • Applications

      Western blotting.

    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.

    Ocm Human
  • View Data Sheet

    Name :

    FLT4 Human

    Description:

    Vascular Endothelial Growth Factor Receptor-3 Human Recombinant

    Tyrosine-protein kinase receptor FLT4, PCL, FLT41, FMS-LIKE TYROSINE KINASE 4, VEGFR-3, VEGFR3.

    Product # :

    PKA-244

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    Quantity :

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    Shipped at Room temp

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    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info

    Description

    Soluble FLT4 Human Recombinant fused with a carboxy-terminal 6X histidine-tag produced in baculovirus is a monomeric, glycosylated, polypeptide containing the extracellular part, 25-774 amino acids and having a total molecular mass of 120 kDa. The soluble receptor protein contains only the first 7 extracellular domains, which contain all the information necessary for ligand binding. The FLT4 is purified by proprietary chromatographic techniques.

    Source

    Insect Cells.

    Formulation

    FLT4 was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its ability to bind recombinant rat VEGF-C in a functional solid phase binding assay. Immobilised recombinant human VEGFR-3/FLT-4 at 5 µg/ml can bind recombinant rat VEGF-C in a linear range of 8-500 ng/ml.

    More Info

    • Introduction

      All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23 aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751 aa residue extracellular domain, a 22 aa transmembrane domain and a 482 aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis.

    • Synonyms

      Tyrosine-protein kinase receptor FLT4, PCL, FLT41, FMS-LIKE TYROSINE KINASE 4, VEGFR-3, VEGFR3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FLT4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FLT4 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 FLT4 in sterile water not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    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.

    Flt4 Human
  • View Data Sheet

    Name :

    GPC4 511 aa Human

    Description:

    Glypican-4 511 aa Human Recombinant

    Glypican 4, Glypican Proteoglycan 4, K-glypican, DJ900E8.1 (Glypican 4), glypican-4.

    Product # :

    PRO-2034

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    Shipped with Ice Packs

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    • description
    • source
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    Description

    Glypican-4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Ala19-Ser529) containing 521 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 58.7kDa.

    Source

    Escherichia Coli.

    Formulation

    Glypican-4 filtered (0.4µm) solution at a concentration of 0.2mg/ml in 20mM Tris buffer, 50mM NaCl, pH 8.0 and 5mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glypican 4, also known as GPC4, is part of a family of glycosylphosphatidylinositol (GPI)-anchored heparan sulphate proteoglycans (HSPGs) which take part in the control of cell division and growth regulation. GPC4 is broadly expressed in human tissues, including lung, kidney, heart, placenta, skeletal muscle, and pancreas. In addition, GPC4 has been shown to be present in astrocytes, haematopoietic-progenitor and bone-marrow-stromal cells.

    • Synonyms

      Glypican 4, Glypican Proteoglycan 4, K-glypican, DJ900E8.1 (Glypican 4), glypican-4.

    • Physical Appearance

      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

      MKHHHHHHASALLAAELKSK SCSEVRRLYV SKGFNKNDAP LHEINGDHLK ICPQGSTCCS QEMEEKYSLQ SKDDFKSVVS EQCNHLQAVF ASRYKKFDEF FKELLENAEK SLNDMFVKTY GHLYMQNSEL FKDLFVELKR YYVVGNVNLE EMLNDFWARL LERMFRLVNS QYHFTDEYLE CVSKYTEQLK PFGDVPRKLK LQVTRAFVAA RTFAQGLAVA GDVVSKVSVV NPTAQCTHAL LKMIYCSHCR GLVTVKPCYN YCSNIMRGCL ANQGDLDFEW NNFIDAMLMV AERLEGPFNI ESVMDPIDVK ISDAIMNMQD NSVQVSQKVF QGCGPPKPLP AGRISRSISE SAFSARFRPH HPEERPTTAA GTSLDRLVTD VKEKLKQAKK FWSSLPSNVC NDERMAAGNG NEDDCWNGKG KSRYLFAVTG NGLANQGNNP EVQVDTSKPD ILILRQIMAL RVMTSKMKNA YNGNDVDFFD ISDESSGEGS GSGCEYQQCP SEFDYNATDH AGKSANEKAD S.

    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.

    Gpc4 511 Aa Human
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