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Search results

1000 results found for “Pregnancy Specific Beta-1-Glycoprotein”

Name

Description

Product #

Price

Quantity

Shipping Method

  • View Data Sheet

    Name :

    CIB1 Antibody

    Description:

    Calcium and Integrin Binding 1, Mouse Anti Human

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

    Product # :

    ANT-377

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    • formulation
    • More Info

    Formulation

    1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

    More Info

    • Introduction

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

    • Synonyms

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

    • Immunogen

      Anti-human CIB1 mAb is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human CIB1 amino acids 1-191 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and κ light chain.

    • Clone

      P1D1AT.

    • Applications

      CIB1 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:1,000 ~ 2,000. Recommended starting dilution is 1:1,000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

      CIB1 antibody was purified from mouse ascitic fluids by protein-G 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.

    Cib1 Antibody
  • View Data Sheet

    Name :

    CCL1 Human

    Description:

    I-309 Human Recombinant (CCL1)

    Small inducible cytokine A1, CCL1, T lymphocyte-secreted protein I-309, chemokine (C-C motif) ligand 1, P500, SISe, TCA3, I-309, SCYA1.

    Product # :

    CHM-312

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

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

    Description

    I-309 Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 74 amino acids and having a molecular mass of 8504 Dalton. The I-309 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CCL1 protein was lyophilized with no additives.

    Purity

    Greater than 99.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The Biological activity is calculated by its ability to chemoattract human T cells at 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 1 (CCL1) is a small glycoprotein secreted by activated T cells that belongs to a family inflammatory cytokines known as chemokines. CCL1 attracts monocytes, NK cells, and immature B cells and dendritic cells by interacting with a cell surface chemokine receptor called CCR8. This chemokine resides in a large cluster of CC chemokines on human chromosome 17.

    • Synonyms

      Small inducible cytokine A1, CCL1, T lymphocyte-secreted protein I-309, chemokine (C-C motif) ligand 1, P500, SISe, TCA3, I-309, SCYA1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized I-309 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL1 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 I-309 in 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 Ser-Lys-Ser-Met-Gln.

    • Background

      What is the molecular weight/Mw of CCL1 HUMAN Protein?
      CCL1 HUMAN Protein has a total Mw of 8.5kDa.

      What is the source or expression system of CCL1 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL1 HUMAN Protein?
      CCL1 HUMAN Protein is >99% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL1 HUMAN Protein?
      The Biological activity is calculated by its ability to chemoattract human T cells at 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

      What is the amino acid sequence of CCL1 HUMAN Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Lys-Ser-Met-Gln.

      What applications can CCL1 HUMAN Protein be used in?
      CCL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL1 HUMAN Protein?
      The endotoxin level is minimal, CCL1 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.

    I 309 Human
  • View Data Sheet

    Name :

    STBD1 Human

    Description:

    Starch Binding Domain 1 Human Recombinant

    Starch Binding Domain 1, Genethonin 1, GENEX3414, Starch-Binding Domain-Containing Protein 1.

    Product # :

    PRO-1545

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    STBD1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 358 amino acids (24-358) and having a molecular mass of 39.1kDa.STBD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The STBD1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      STBD1 has one carbohydrate binding type-20 (CBM20) domain and has the ability to bind to carbohydrates. STBD1 is highly expressed in cardiac and skeletal muscles.

    • Synonyms

      Starch Binding Domain 1, Genethonin 1, GENEX3414, Starch-Binding Domain-Containing Protein 1.

    • 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 MGSRGGPGDT GKDGDAEQEK DAPLGGAAIP GGHQSGSSGL SPGPSGQELV TKPEHLQESN GHLISKTKDL GKLQAASWRL QNPSREVCDN SREHVPSGQF PDTEAPATSE TSNSRSYSEV SRNESLESPM GEWGFQKGQE ISAKAATCFA EKLPSSNLLK NRAKEEMSLS DLNSQDRVDH EEWEMVPRHS SWGDVGVGGS LKAPVLNLNQ GMDNGRSTLV EARGQQVHGK MERVAVMPAG SQQVSVRFQV HYVTSTDVQF IAVTGDHECL GRWNTYIPLH YNKDGFWSHS IFLPADTVVE WKFVLVENGG VTRWEECSNR FLETGHEDKV VHAWWGIH

    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.

    Stbd1 Human
  • View Data Sheet

    Name :

    TK1 Human

    Description:

    Thymidine Kinase 1 Human Recombinant

    Thymidine kinase 1 soluble, thymidine kinase cytosolic, TK2, EC 2.7.1.21.

    Product # :

    PKA-036

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    TK1 Human Recombinant produced in E. coli is a single polypeptide chain containing 258 amino acids (1-234) and having a molecular mass of 28.0 kDa.TK1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TK1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Thymidine Kinase 1 (TK1) is a phosphotransferase (a kinase): 2'-deoxythymidine kinase, ATP-thymidine 5'-phosphotransferase. TK1 is present in 2 forms in mammalian cells, TK1 and TK2. Thymidine kinases hold a main function in the synthesis of DNA and thus in cell division, as they are part of the distinctive reaction chain to introduce deoxythymidine (present in the body fluids as a result of degradation of DNA from food and from dead cells) into the DNA. Thymidine kinase is necessary for the action of many antiviral drugs. Thymidine kinase is used to select hybridoma cell lines in production of monoclonal antibodies.

    • Synonyms

      Thymidine kinase 1 soluble, thymidine kinase cytosolic, TK2, EC 2.7.1.21.

    • 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 MGSHMSCINL PTVLPGSPSK TRGQIQVILG PMFSGKSTEL MRRVRRFQIA QYKCLVIKYA KDTRYSSSFC THDRNTMEAL PACLLRDVAQ EALGVAVIGI DEGQFFPDIV EFCEAMANAG KTVIVAALDG TFQRKPFGAI LNLVPLAESV VKLTAVCMEC FREAAYTKRL GTEKEVEVIG GADKYHSVCR LCYFKKASGQ PAGPDNKENC PVPGKPGEAV AARKLFAPQQ ILQCSPAN.

    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.

    Tk1 Human
  • View Data Sheet

    Name :

    HSA Protein

    Description:

    HSA Human Protein

    HSA, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.

    Product # :

    PRO-354

    Price :

    Quantity :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    HSA contains 584 amino acid residues derived from the prototypicalHSA sequence.

    Source

    Human Serum.

    Formulation

    0.2gr/ml solution containing no additives.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HSA is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted HSA. HSA is a soluble, monomeric protein which comprises about one-half of the blood serum protein. HSA functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and plays a role in stabilizing extracellular fluid volume. Mutations in this gene on chromosome 4 result in various anomalous proteins. HSA is a globular unglycosylated serum protein of molecular weight 65,000. The human HSA gene is 16,961 nucleotides long from the putative 'cap' site to the first poly (A) addition site. It is split into 15 exons which are symmetrically placed within the 3 domains that are thought to have arisen by triplication of a single primordial domain.
      HSA is widely used to stabilize blood volume generally from donors but the fear of contamination such as HIV & Hepatitis has enticed great interest in the recombinant form which is identical to the natural blood.
      Suitable for use in biochemical, excipient (an inert substance used as a diluent or vehicle for a drug), culture media and chromatographic applications.

    • Synonyms

      HSA, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.

    • Physical Appearance

      Sterile Filtered clear yellowish solution.

    • Stability

      HSA although stable at room temperature for 2 weeks should be stored at 4°C.

    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.

    Human Serum Albumin
  • View Data Sheet

    Name :

    BD 2 Human

    Description:

    Beta Defensin-2 Human Recombinant

    BD-2, hBD-2, Defensin beta 2, Skin-antimicrobial peptide 1, SAP1, DEFB4, DEFB102, DEFB2, DEFB4P, Beta-defensin 2.

    Product # :

    CYT-571

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    Description

    Beta Defensin-2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 41 amino acids and having a molecular mass of 4.3 kDa. The BD-2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Human BD-2 was lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution containing 20mM PB pH-7.4 and 130mM NaCl.

    Purity

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

    Biological Activity

    Determined by the ability to chemoattract human dendritic immature cells at a concentration of 10-100ng/ml.

    More Info

    • Synonyms

      BD-2, hBD-2, Defensin beta 2, Skin-antimicrobial peptide 1, SAP1, DEFB4, DEFB102, DEFB2, DEFB4P, Beta-defensin 2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      GIGDPVTCLK SGAICHPVFC PRRYKQIGTC GLPGTKCCKK P.

    • Background

      Beta Defensin-2 Human Recombinant: Unveiling its Role in Innate Immunity and Therapeutic Potential

      Abstract:


      Beta Defensin-2 (BD-2), a member of the defensin family, plays a crucial role in innate immunity and host defense. This research paper provides an overview of BD-2 human recombinant, exploring its molecular characteristics, antimicrobial properties, and therapeutic applications. Understanding the multifaceted role of BD-2 offers new avenues for developing innovative immunotherapies. This article offers a concise analysis of BD-2, highlighting its impact on innate immunity and its therapeutic potential.

      Introduction:


      Innate immunity serves as the first line of defense against invading pathogens. BD-2, a key antimicrobial peptide within the defensin family, plays a vital role in immune responses at epithelial surfaces. This paper provides an overview of BD-2, shedding light on its structure, function, and therapeutic potential.

      BD-2 Structure and Function:


      BD-2 is a cationic peptide that exhibits a conserved cysteine motif, conferring its antimicrobial activity. It acts by disrupting microbial cell membranes, exerting a broad spectrum of antimicrobial effects against bacteria, fungi, and viruses. Additionally, BD-2 possesses immunomodulatory properties, regulating inflammatory responses and promoting wound healing.

      Antimicrobial Properties and Therapeutic Applications:


      BD-2 demonstrates potent antimicrobial activity against a wide range of pathogens, including drug-resistant strains. Its ability to combat biofilm formation and enhance immune cell recruitment makes it a promising candidate for developing novel antimicrobial therapies. Furthermore, BD-2's immunomodulatory effects hold potential in treating inflammatory disorders.

      Therapeutic Potential of BD-2 Human Recombinant:


      BD-2 human recombinant offers exciting prospects in immunotherapy. Strategies aimed at enhancing BD-2 expression or delivering exogenous BD-2 may boost innate immune responses in individuals with compromised immunity or chronic infections. BD-2-based therapeutics could be developed for wound healing, infectious diseases, and inflammatory conditions.

      Challenges and Future Directions:


      While BD-2 shows great promise, challenges remain. Further research is needed to optimize delivery methods of BD-2 and evaluate its safety and efficacy in clinical settings. Understanding the interplay between BD-2 and other immune factors will enable the development of synergistic therapies for enhanced therapeutic outcomes.

      Conclusion:


      BD-2 human recombinant represents a promising avenue for developing novel immunotherapies and combating antimicrobial resistance. Understanding the molecular mechanisms and functional implications of BD-2 in innate immunity opens new horizons for innovative treatments. Continued research in this field has the potential to revolutionize immunotherapy and improve patient outcomes.

      What is the molecular weight/Mw of BD2 Protein?
      BD2 Protein has a total Mw of 4.3kDa.

      What is the source or expression system of BD2 Protein?
      Escherichia Coli.

      What is the Purity of BD2 Protein?
      BD2 Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of BD2 Protein?
      Determined by the ability to chemoattract human dendritic immature cells at a concentration of 10-100ng/ml.

      What is the amino acid sequence of BD2 Protein?
      GIGDPVTCLK SGAICHPVFC PRRYKQIGTC GLPGTKCCKK P.

      What applications can BD2 Protein be used in?
      BD2 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BD2 Protein?
      The endotoxin level is minimal, BD2 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.

    Hbd 2 Human
  • View Data Sheet

    Name :

    GYG1 Human

    Description:

    Glycogenin-1 Human Recombinant

    Glycogenin-1, GYG1, GYG.

    Product # :

    ENZ-431

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    Description

    GYG1 Human Recombinant fused with a 32 amino acid His-T7 tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 365 amino acids (1-333 a.a.) and having a molecular mass of 41.2kDa.The GYG1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GYG1 solution contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glycogenin-1 (GYG1) is an enzyme involved in glycogen biosynthesis. GYG1 is the chief enzyme involved in glycogen polymerisation. Glycogenin-1 is vital for the function of self-glucosylates, using an inter-subunit mechanism, to form an oligosaccharide primer which acts as substrate for glycogen synthase. In addition, GYG1 has a role in regulating glycogen metabolism and the achievement of maximal glycogen levels in skeletal muscle. GYG1 mRNA and protein content and activity increase in the muscle during recovery from prolonged and exhaustive exercise. GYG1 is inactivated with glycogen catabolism which concurs with an increase in glycogenin gene expression as exercise and glycogenolysis advance. Glycogenin will remain covalently attached to the reducing end of the glycogen molecule.

    • Synonyms

      Glycogenin-1, GYG1, GYG.

    • 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

      MHHHHHHMAS MTGGQQMGRD LYDDDDKDRW GSMTDQAFVT LTTNDAYAKG ALVLGSSLKQ HRTTRRLVVL ATPQVSDSMR KVLETVFDEV IMVDVLDSGD SAHLTLMKRP ELGVTLTKLH CWSLTQYSKC VFMDADTLVL ANIDDLFDRE ELSAAPDPGW PDCFNSGVFV YQPSVETYNQ LLHLASEQGS FDGGDQGILN TFFSSWATTD IRKHLPFIYN LSSISIYSYL PAFKVFGASA KVVHFLGRVK PWNYTYDPKT KSVKSEAHDP NMTHPEFLIL WWNIFTTNVL PLLQQFGLVK DTCSYVNVED VSGAISHLSL GEIPAMAQPF VSSEERKERW EQGQADYMGA DSFDNIKRKL DTYLQ.

    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.

    Gyg1 Human
  • View Data Sheet

    Name :

    FUCA1 Human

    Description:

    Fucosidase Alpha-L- 1 Plasma Human Recombinant

    Fucosidase, Alpha-L- 1, Tissue, Alpha-L-Fucoside Fucohydrolase 1, Alpha-L-Fucosidase 1, Alpha-L-Fucosidase I, EC 3.2.1.51, Tissue Alpha-L-Fucosidase, EC 3.2.1, FUCA, Tissue alpha-L-fucosidase.

    Product # :

    ENZ-921

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    Description

    FUCA1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 445 amino acids (28-466a.a.) and having a molecular mass of 51.7kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). FUCA1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    FUCA1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Fucosidase Alpha-L- 1 Plasma, also known as FUCA1 is a member of the glycosyl hydrolase 29 family which is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Fucosidosis is an autosomal recessive lysosomal storage disease caused by the absence of alpha-L-fucosidase activity.

    • Synonyms

      Fucosidase, Alpha-L- 1, Tissue, Alpha-L-Fucoside Fucohydrolase 1, Alpha-L-Fucosidase 1, Alpha-L-Fucosidase I, EC 3.2.1.51, Tissue Alpha-L-Fucosidase, EC 3.2.1, FUCA, Tissue alpha-L-fucosidase.

    • 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

      VRRAQPPRRY TPDWPSLDSR PLPAWFDEAK FGVFIHWGVF SVPAWGSEWF WWHWQGEGRP QYQRFMRDNY PPGFSYADFG PQFTARFFHP EEWADLFQAA GAKYVVLTTK HHEGFTNWPS PVSWNWNSKD VGPHRDLVGE LGTALRKRNI RYGLYHSLLE WFHPLYLLDK KNGFKTQHFV SAKTMPELYD LVNSYKPDLI WSDGEWECPD TYWNSTNFLS WLYNDSPVKD EVVVNDRWGQ NCSCHHGGYY NCEDKFKPQS LPDHKWEMCT SIDKFSWGYR RDMALSDVTE ESEIISELVQ TVSLGGNYLL NIGPTKDGLI VPIFQERLLA VGKWLSINGE AIYASKPWRV QWEKNTTSVW YTSKGSAVYA IFLHWPENGV LNLESPITTS TTKITMLGIQ GDLKWSTDPD KGLFISLPQL PPSAVPAEFA WTIKLTGVKH 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.

    Fuca1 Human
  • View Data Sheet

    Name :

    HP-NAP

    Description:

    Neutrophil-activating protein A Helicobacter Pylori Recombinant

    DNA protection during starvation protein, Bacterioferritin, HP-NAP, Neutrophil-activating protein A, NAP A, dps, napA.

    Product # :

    PRO-2035

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    Description

    HP-NAP Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Met1-Ala144) containing 154 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 18.2kDa.

    Source

    Escherichia Coli.

    Formulation

    HP-NAP was filtered (0.4 µm) and lyophilized in 20mM Tris buffer and 50mM NaCl, pH 7.5.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HP-NAP protects DNA from oxidative damage by sequestering intracellular Fe2+ ion and storing it in the form of Fe3+ oxyhydroxide mineral. One hydrogen peroxide oxidizes two Fe2+ ions, thus preventing hydroxyl radical production by the Fenton reaction. HP-NAP is necessary for the survival in the presence of oxidative stress. Dps is also a virulence factor which activates neutrophils, mast cells and monocytes. HP-NAP binds to neutrophil-glycosphingolipids and to sulfated carbohydrates on mucin. HP-NAP might play a part in the accumulation of neutrophils and monocytes at the site of infection. HP-NAP induces superoxide anion generation, adhesion and chemotaxis of neutrophils, via a pertussis toxin-sensitive pathway involving MAP kinases.

    • Synonyms

      DNA protection during starvation protein, Bacterioferritin, HP-NAP, Neutrophil-activating protein A, NAP A, dps, napA.

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

    • Amino Acid Sequence

      MKHHHHHHASMKTFEILKHL QADAIVLFMK VHNFHWNVKG TDFFNVHKAT EEIYEEFADM FDDLAERIVQ LGHHPLVTLS EAIKLTRVKE ETKTSFHSKD IFKEILEDYK YLEKEFKELS NTAEKEGDKV TVTYADDQLA KLQKSIWMLQ AHLA.

    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.

    Hp Nap
  • View Data Sheet

    Name :

    PKIB Human

    Description:

    Protein Kinase Inhibitor Beta Human Recombinant

    cAMP-dependent protein kinase inhibitor beta, PKI-beta, PKIB, PRKACN2, FLJ23817.

    Product # :

    PKA-003

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    Description

    PKIB Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 98 amino acids (1-78) and having a molecular mass of 10.6kDa (Molecular size on SDS-PAGE will appear higher). PKIB is fused to a 20 aa His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      cAMP-dependent protein kinase inhibitor beta (PKIB) belongs to the cAMP-dependent protein kinase inhibitor family. PKIB may interact with the catalytic subunit of cAMP-dependent protein kinase and function as a competitive inhibitor.

    • Synonyms

      cAMP-dependent protein kinase inhibitor beta, PKI-beta, PKIB, PRKACN2, FLJ23817.

    • 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 MRTDSSKMTD VESGVANFAS SARAGRRNAL PDIQSSAATD GTSDLPLKLE ALSVKEDAKE KDEKTTQDQL EKPQNEEK.

    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.

    Pkib Human
  • View Data Sheet

    Name :

    TULP1 Human

    Description:

    Tubby Like Protein 1 Human Recombinant

    Tubby like protein 1, TUBL1, RP14, LCA15, tubby-related protein 1.

    Product # :

    PRO-1191

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    Description

    TULP1 Human Recombinant produced in E. coli is a single polypeptide chain containing 276 amino acids (290-542) and having a molecular mass of 31.1 kDa.TULP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TULP1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 5mM DTT, 2mM EDTA and 50% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tubby-related protein 1 (TULP1) belongs to the TULP family of 4 proteins (TUB and TULP1, -2, and -3), categorized structurally by the highly conserved C-terminal half of the protein. Tubby-like gene family (TULPs) members are found in plants, vertebrates, and invertebrates and encode proteins of unknown function. TULP proteins share a conserved C-terminal region of roughly 200 amino acid residues. In the retina, TULP1 is observed exclusively in the photoreceptor cells, localizing predominantly in the inner segments and connecting cilium and to a lesser degree in the perinuclear cytoplasm and synaptic termini. TULP1 gene mutations are linked with retinitis pigmentosa.

    • Synonyms

      Tubby like protein 1, TUBL1, RP14, LCA15, tubby-related 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 MGSEPREFVL RPAPQGRTVR CRLTRDKKGM DRGMYPSYFL HLDTEKKVFL LAGRKRKRSK TANYLISIDP TNLSRGGENF IGKLRSNLLG NRFTVFDNGQ NPQRGYSTNV ASLRQELAAV IYETNVLGFR GPRRMTVIIP GMSAENERVP IRPRNASDGL LVRWQNKTLE SLIELHNKPP VWNDDSGSYT LNFQGRVTQA SVKNFQIVHA DDPDYIVLQF GRVAEDAFTL DYRYPLCALQ AFAIALSSFD GKLACE

    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.

    Tulp1 Human
  • View Data Sheet

    Name :

    ICAM-1 Human

    Description:

    Intercellular Adhesion Molecule-1 Human Recombinant

    Intercellular adhesion molecule 1, ICAM-1, Major group rhinovirus receptor, CD54 antigen, ICAM1, BB2, CD54, P3.58.

    Product # :

    PRO-383

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    Description

    ICAM-1 Human Recombinant is expressed in E. coli containing 455 amino acids 28-483 fused to an amino terminal hexahistidine tag.The ICAM-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ICAM-1 is supplied (0.2mg/ml) in PBS, 50% Glycerol, 2mM Imidazole.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      ICAM-1 also called CD54 is a single chain membrane glycoprotein expressed on the surface of a variety of non-haematopoietic and haematopoietic cell types and has roles in signal transduction, cell signaling and lymphocyte adhesion. ICAM1 binds to integrins such as CD11a / CD18, or CD11b / CD18. ICAM1 is also used by Rhinovirus as a receptor. ICAM-1 is an intercellular adhesion molecule constantly present in low concentrations in the membranes of leukocytes and endothelial cells. When stimulated by cytokine the concentrations significantly increase. ICAM-1 can be stimulated by interleukin-1 (IL-1) and tumor necrosis factor alpha (TNFA) and is expressed by the vascular endothelium, macrophages and lymphocytes. ICAM-1 is a ligand for LFA-1 which is a receptor found on leukocytes. Upon activation, leukocytes bind to endothelial cells via ICAM-1/LFA-1 and then transmigrate into tissues.
      ICAM-1 is implicated in subarachnoid hemorrhage (SAH). Levels of ICAM-1 are shown to be notably elevated in patients with SAH.
      Soluble ICAM-1 is detectable in the plasma and is elevated in patients with various inflammatory conditions.

    • Synonyms

      Intercellular adhesion molecule 1, ICAM-1, Major group rhinovirus receptor, CD54 antigen, ICAM1, BB2, CD54, P3.58.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

    • Applications

      ICAM-I can be used directly as a positive control in Western blotting, ELISA, immunoprecipitation and other immunological experiments.
      The biological activity of this product has not yet been tested.

    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.

    Icam 1 Human
  • View Data Sheet

    Name :

    LGALS4 Human

    Description:

    Galectin-4 Human Recombinant

    Galectin-4, Gal-4, Lactose-binding lectin 4, L-36 lactose-binding protein, L36LBP, Antigen NY-CO-27, LGALS4, lectin galactoside-binding soluble 4, GAL4.

    Product # :

    CYT-686

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    • sds-page

    Description

    Galectin-4 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 343 amino acids (1-323 a.a.) and having a molecular mass of 38.1kDa.Galectin-4 is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LGALS4 protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    sds-page

    LGALS4 Human-SDS-PAGE - Product image 1

    More Info

    • Introduction

      Galectin-4 is a member of the subfamily of galectins composed of two carbohydrate recognition domains having similar peptide chains. The galectins are a family of beta-galactoside-binding proteins having a role in modulating cell-cell and cell-matrix interactions, which inhibits chronic inflammations, GVHD, and allergic responses. LGALS4 expression is limited to small intestine, colon, and rectum, and it is underexpressed in colorectal cancer. LGALS4 binds as an endogenous ligand to glycosphingolipids having 3-O-sulfated Gal residues and bind as well to cholesterol-3-sulfate. LGALS4 takes part in cell adhesion. LGALS4 plays a role in crosslinking the lateral cell membranes of the surface-lining epithelial cells, thus supporting epithelial integrity against mechanical stress exerted by the bowel lume. LGALS4 is in charge of intestinal inflammation via selective regulation of peripheral and mucosal T-cell cell cycle, in addition to cell death by apoptosis of T-cells by a pathway independent of the activation of caspases. LGALS4 blockade decreases TNF-alpha inhibitor induced T-cell death. LGALS4 decreases pro-inflammatory cytokine secretion including IL-6 & IL-17.

    • Synonyms

      Galectin-4, Gal-4, Lactose-binding lectin 4, L-36 lactose-binding protein, L36LBP, Antigen NY-CO-27, LGALS4, lectin galactoside-binding soluble 4, GAL4.

    • 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 MAYVPAPGYQ PTYNPTLPYY QPIPGGLNVG MSVYIQGVAS EHMKRFFVNF VVGQDPGSDV AFHFNPRFDG WDKVVFNTLQ GGKWGSEERK RSMPFKKGAA FELVFIVLAE HYKVVVNGNP FYEYGHRLPL QMVTHLQVDG DLQLQSINFI GGQPLRPQGP PMMPPYPGPG HCHQQLNSLP TMEGPPTFNP PVPYFGRLQG GLTARRTIII KGYVPPTGKS FAINFKVGSS GDIALHINPR MGNGTVVRNS LLNGSWGSEE KKITHNPFGP GQFFDLSIRC GLDRFKVYAN GQHLFDFAHR LSAFQRVDTL EIQGDVTLSY VQI.

    • Background

      What is the molecular weight/Mw of LGALS4 HUMAN Protein?
      LGALS4 HUMAN Protein has a total Mw of 38.1kDa.

      What is the source or expression system of LGALS4 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of LGALS4 HUMAN Protein?
      LGALS4 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of LGALS4 HUMAN Protein?
      The biological functionality of LGALS4 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of LGALS4 HUMAN Protein?
      MGSSHHHHHH SSGLVPRGSH MAYVPAPGYQ PTYNPTLPYY QPIPGGLNVG MSVYIQGVAS EHMKRFFVNF VVGQDPGSDV AFHFNPRFDG WDKVVFNTLQ GGKWGSEERK RSMPFKKGAA FELVFIVLAE HYKVVVNGNP FYEYGHRLPL QMVTHLQVDG DLQLQSINFI GGQPLRPQGP PMMPPYPGPG HCHQQLNSLP TMEGPPTFNP PVPYFGRLQG GLTARRTIII KGYVPPTGKS FAINFKVGSS GDIALHINPR MGNGTVVRNS LLNGSWGSEE KKITHNPFGP GQFFDLSIRC GLDRFKVYAN GQHLFDFAHR LSAFQRVDTL EIQGDVTLSY VQI.

      What applications can LGALS4 HUMAN Protein be used in?
      LGALS4 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for LGALS4 HUMAN Protein?
      The endotoxin level is minimal, LGALS4 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.

    Lgals4 Human
  • View Data Sheet

    Name :

    BDNF Human

    Description:

    Brain-Derived Neurotrophic Factor Human Recombinant

    Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

    Product # :

    CYT-207

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    • Activity

    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

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

    Activity

    bdnf activity - Product image 1

    More Info

    • Introduction

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

    • Synonyms

      Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

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

    • Background

      Final Thoughts

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

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

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

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

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

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

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

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

    • Protein content

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

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    Bdnf Human
  • View Data Sheet

    Name :

    CTRB1 Human

    Description:

    Chymotrypsinogen-B1, Human Recombinant

    Product # :

    ENZ-1016

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    Description

    Recombinant Human CTRB1 expressed in E.coli containing 245 amino acids having a Mw of 27kDa is purified by standard chromatography techniques.

    Source

    E.coli

    Formulation

    The Human CTRB1 was lyophilized without any additives.

    Purity

    Greater than 95% as determined by HPLC.

    Biological Activity

    1100 units/mg protein.
    One unit is defined as the amount of enzyme that will hydrolyze 1.0 μmole of N-alpha-acetyl-L-tyrosine ethyl ester (ATEE) per min at pH 7.0 at 25°C.

    More Info

    • Introduction

      Chymotrypsinogen-B1 (CTRB1) belongs to the serine protease family of enzymes and forms a main precursor of the pancreatic proteolytic enzymes. CTRB1 is located next to a related chymotrypsinogen gene. CTRB1 is a protein coding gene which encodes different isoforms which may undergo similar processing to generate the mature protein.

    • Physical Appearance

      Sterile Filtered lyophilized powder.

    • Stability

      Recombinant Human CTRB1 although stable at room temp for 1 week, should be stored desiccated 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 Human CTRB1 in 1ml 50mM HAc which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      CG VPAIHPVLSG LSRIVNGEDA VPGSWPWQVS LQDKTGFHFC GGSLISEDWV VTAAHCGVRT SDVVVAGEFD QGSDEENIQV LKIAKVFKNP KFSILTVNND ITLLKLATPA RFSQTVSAVC LPSADDDFPAGTLCATTGWG KTKYNANKTP DKLQQAALPL LSNAECKKSW GRRITDVMIC AGASGVSSCM GDSGGPLVCQ KDGAWTLVGI VSWGSDTCST SSPGVYARVTKLIPWVQKIL AAN.

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    Ctrb1 Human
  • View Data Sheet

    Name :

    PLGF Human, HEK

    Description:

    Placental Growth Factor Human Recombinant

    PIGF, PGF, PLGF-1

    Product # :

    CYT-1193

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    Description

    PLGF Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 21-170) containing 160 amino acids and having a molecular mass of 18.3kDa.PLGF is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    PLGF protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Placental Growth Factor (PLGF) which is a member of the VEGF sub-family, is a growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration. PLGFmainly plays a role in trophoblast growth and differentiation and binds to receptor vegfr-1/flt1.

    • Synonyms

      PIGF, PGF, PLGF-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

      DGSMAVPPQQ WALSAGNGSS EVEVVPFQEV WGRSYCRALE RLVDVVSEYP SEVEHMFSPS CVSLLRCTGC CGDENLHCVP VETANVTMQL LKIRSGDRPS YVELTFSQHV RCECRPLREK MKPERRRPKG RGKRRREKQR PTDCHLCGDA VPRRHHHHHH

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    Plgf Human
  • View Data Sheet

    Name :

    GDI2 Human

    Description:

    GDP Dissociation Inhibitor 2 Human Recombinant

    GDP Dissociation Inhibitor 2, GDI2, RABGDIB, Guanosine Diphosphate Dissociation Inhibitor 2 , Rab GDI Beta , GDI-2, Epididymis Secretory Sperm Binding Protein Li 46e, Rab GDP Dissociation Inhibitor Beta , Rab GDP-Dissociation , HEL-S-46e.

    Product # :

    PRO-1948

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    Description

    GDI2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 468 amino acids (1-445) and having a molecular mass of 53.1 kDa.GDI2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GDI2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Rab GDP dissociation inhibitor beta isoform 1 (GDI2) is a member of the GDP dissociation inhibitors (GDIs) family. GDI proteins can bind and release GDP-bound Rab proteins from membranes. GDI1 interacts with virtually all of the Rab proteins, whereas GDI2 interacts with Rabll but not Rab3A. GDI2 distributes ubiquitously, presenting a membrane bound location in perinuclear regions of cells.

    • Synonyms

      GDP Dissociation Inhibitor 2, GDI2, RABGDIB, Guanosine Diphosphate Dissociation Inhibitor 2 , Rab GDI Beta , GDI-2, Epididymis Secretory Sperm Binding Protein Li 46e, Rab GDP Dissociation Inhibitor Beta , Rab GDP-Dissociation , HEL-S-46e.

    • 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 MGSMNEEYDV IVLGTGLTEC ILSGIMSVNG KKVLHMDRNP YYGGESASIT PLEDLYKRFK IPGSPPESMG RGRDWNVDLI PKFLMANGQL VKMLLYTEVT RYLDFKVTEG SFVYKGGKIY KVPSTEAEAL ASSLMGLFEK RRFRKFLVYV ANFDEKDPRT FEGIDPKKTT MRDVYKKFDL GQDVIDFTGH ALALYRTDDY LDQPCYETIN RIKLYSESLA RYGKSPYLYP LYGLGELPQG FARLSAIYGG TYMLNKPIEE IIVQNGKVIG VKSEGEIARC KQLICDPSYV KDRVEKVGQV IRVICILSHP IKNTNDANSC QIIIPQNQVN RKSDIYVCMI SFAHNVAAQG KYIAIVSTTV ETKEPEKEIR PALELLEPIE QKFVSISDLL VPKDLGTESQ IFISRTYDAT THFETTCDDI KNIYKRMTGS EFDFEEMKRK KNDIYGED.

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    Gdi2 Human
  • View Data Sheet

    Name :

    CES1 Human

    Description:

    Carboxylesterase 1 Human Recombinant

    Liver carboxylesterase 1 isoform a, CES1, ACAT, CE-1, CEH, CES2, hCE-1, HMSE, HMSE1, PCE-1, REH, SES1, TGH, Acyl-coenzyme A:cholesterol acyltransferase, Brain carboxylesterase hBr1.

    Product # :

    ENZ-1099

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    Description

    CES1 Human produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 559 amino acids (19-568 a.a.) and having a molecular mass of 61.7kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).CES1 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CES1 protein solution (0.5mg/ml) contains 25mM Sodium Acetate (pH 4.0), 10% glycerol, 0.1M NaCl and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CES1 is a part of the alpha/beta fold hydrolase familyand participates in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. CES1hydrolyzes aromatic and aliphatic esters, although it has no catalytic activity toward amides or a fatty acyl-CoA ester. CES1hydrolyzes the methyl ester group of cocaine to form benzoylecgonine and catalyzes the transesterification of cocaine to form cocaethylene. CES1also plays a role in detoxification in the lung and protection of the central nervous system from ester or amide compounds.CES1 is found in most tissues, mainly in the liver.

    • Synonyms

      Liver carboxylesterase 1 isoform a, CES1, ACAT, CE-1, CEH, CES2, hCE-1, HMSE, HMSE1, PCE-1, REH, SES1, TGH, Acyl-coenzyme A:cholesterol acyltransferase, Brain carboxylesterase hBr1.

    • 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

      ADLGHPSSPP VVDTVHGKVL GKFVSLEGFA QPVAIFLGIP FAKPPLGPLR FTPPQPAEPW
      SFVKNATSYP PMCTQDPKAG QLLSELFTNR KENIPLKLSE DCLYLNIYTP ADLTKKNRLP
      VMVWIHGGGL MVGAASTYDG LALAAHENVV VVTIQYRLGI WGFFSTGDEH SRGNWGHLDQ
      VAALRWVQDN IASFGGNPGS VTIFGESAGG ESVSVLVLSP LAKNLFHRAI SESGVALTSV
      LVKKGDVKPL AEQIAITAGC KTTTSAVMVH CLRQKTEEEL LETTLKMKFL SLDLQGDPRE
      SQPLLGTVID GMLLLKTPEE LQAERNFHTV PYMVGINKQE FGWLIPMQLM SYPLSEGQLD
      QKTAMSLLWK SYPLVCIAKE LIPEATEKYL GGTDDTVKKK DLFLDLIADV MFGVPSVIVA
      RNHRDAGAPT YMYEFQYRPS FSSDMKPKTV IGDHGDELFS VFGAPFLKEG ASEEEIRLSK
      MVMKFWANFA RNGNPNGEGL PHWPEYNQKE GYLQIGANTQ AAQKLKDKEV AFWTNLFAKK AVEKPPQTEH IELHHHHHH.

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    Ces1 Human
  • View Data Sheet

    Name :

    SERPINF2 Mouse

    Description:

    Serpin Peptidase Inhibitor, Clade F Member 2 Mouse Recombinant

    Alpha-2-antiplasmin, Alpha-2-AP, Alpha-2-plasmin inhibitor, Alpha-2-PI, Serpin F2.

    Product # :

    PRO-2240

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    Description

    SERPINF2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 470 amino acids (28-491 a.a.) and having a molecular mass of 52.9kDa (Migrates at 70-100kDa on SDS-PAGE under reducing conditions). SERPINF2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    SERPINF2 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Alpha-2-antiplasmin (SERPINF2) is a serine protease inhibitor. The main targets of SERPINF2 are plasmin and trypsin; however SERPINF2 also inactivates matriptase-3/TMPRSS7 and chymotrypsin.

    • Synonyms

      Alpha-2-antiplasmin, Alpha-2-AP, Alpha-2-plasmin inhibitor, Alpha-2-PI, Serpin F2.

    • 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

      VDLPGQQPVS EQAQQKLPLP ALFKLDNQDF GDHATLKRSP GHCKSVPTAE ETRRLAQAMM AFTTDLFSLV AQTSTSSNLV LSPLSVALAL SHLALGAQNQ TLHSLHRVLH MNTGSCLPHL LSHFYQNLGP GTIRLAARIY LQKGFPIKDD FLEQSERLFG AKPVKLTGKQ EEDLANINQW VKEATEGKIE DFLSELPDST VLLLLNAIHF HGFWRTKFDP SLTQKDFFHL DERFTVSVDM MHAVSYPLRW FLLEQPEIQV AHFPFKNNMS FVVVMPTYFE WNVSEVLANL TWDTLYHPSL QERPTKVWLP KLHLQQQLDL VATLSQLGLQ ELFQGPDLRG ISEQNLVVSS VQHQSTMELS EAGVEAAAAT SVAMNRMSLS SFTVNRPFLF FIMEDTIGVP LFVGSVRNPN PSALPQLQEQ RDSPDNRLIG QNDKADFHGG KTFGPDLKLA PRMEEDYPQF SSPKHHHHHH.

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    Serpinf2 Mouse
  • View Data Sheet

    Name :

    GBA3 Human

    Description:

    Glucosidase Beta Acid 3 Human Recombinant

    Cytosolic beta-glucosidase, Cytosolic beta-glucosidase-like protein 1, GBA3, CBG, CBGL1, Glucosidase Beta Acid 3, GH1, Glycoside Hydrolase Family 1, GLUC, KLRP.

    Product # :

    ENZ-831

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    Description

    GBA3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 492 amino acids (1-469 a.a.) and having a molecular mass of 56.1kDa.GBA3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    GBA3 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glucosidase Beta Acid 3, also known as GBA3, hydrolyzes various types of glycosides. GBA3 takes part in a nonlysosomal catabolic pathway of glycosylceramide. GBA3 is a protein coding gene which acts as beta-glycosylceramidase.

    • Synonyms

      Cytosolic beta-glucosidase, Cytosolic beta-glucosidase-like protein 1, GBA3, CBG, CBGL1, Glucosidase Beta Acid 3, GH1, Glycoside Hydrolase Family 1, GLUC, KLRP.

    • 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 MGSMAFPAGF GWAAATAAYQ VEGGWDADGK GPCVWDTFTH QGGERVFKNQ TGDVACGSYT LWEEDLKCIK QLGLTHYRFS LSWSRLLPDG TTGFINQKGI DYYNKIIDDL LKNGVTPIVT LYHFDLPQTL EDQGGWLSEA IIESFDKYAQ FCFSTFGDRV KQWITINEAN VLSVMSYDLG MFPPGIPHFG TGGYQAAHNL IKAHARSWHS YDSLFRKKQK GMVSLSLFAV WLEPADPNSV SDQEAAKRAI TFHLDLFAKP IFIDGDYPEV VKSQIASMSQ KQGYPSSRLP EFTEEEKKMI KGTADFFAVQ YYTTRLIKYQ ENKKGELGIL QDAEIEFFPD PSWKNVDWIY VVPWGVCKLL KYIKDTYNNP VIYITENGFP QSDPAPLDDT QRWEYFRQTF QELFKAIQLD KVNLQVYCAW SLLDNFEWNQ GYSSRFGLFH VDFEDPARPR VPYTSAKEYA KIIRNNGLEA HL.

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    Gba3 Human
  • View Data Sheet

    Name :

    PF4V1 Human

    Description:

    Platelet Factor 4 Variant 1 Human Recombinant

    PF4V1, Platelet Factor 4 Variant 1, CXCL4L1, CXCL4V1, PF4alt, PF4var1, SCYB4V1, PF4-ALT, PF4A, C-X-C Motif Chemokine 4, Platelet Factor 4 Variant, Platelet Factor 4, Variant 1 (PF4-Like) , C-X-C Motif Chemokine 4 Variant.

    Product # :

    CHM-027

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    Description

    PF4V1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 97 amino acids (31-104 a.a.) and having a molecular mass of 10.6kDa.PF4V1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PF4V1 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Platelet Factor 4 Variant 1 (PF4V1) is a member of the intercrine alpha (chemokine CxC) family. PF4V1 is an inhibitor of angiogenesis and inhibitor of endothelial cell chemotaxis (in vitro).

    • Synonyms

      PF4V1, Platelet Factor 4 Variant 1, CXCL4L1, CXCL4V1, PF4alt, PF4var1, SCYB4V1, PF4-ALT, PF4A, C-X-C Motif Chemokine 4, Platelet Factor 4 Variant, Platelet Factor 4, Variant 1 (PF4-Like) , C-X-C Motif Chemokine 4 Variant.

    • Physical Appearance

      Sterile Filtered colorless clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSFARAEAE EDGDLQCLCV KTTSQVRPRH ITSLEVIKAG PHCPTAQLIA TLKNGRKICL DLQALLYKKI IKEHLES.

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    Pf4V1 Human
  • View Data Sheet

    Name :

    EREG Human, His

    Description:

    Epiregulin Human Recombinant, His Tag

    Epiregulin, Proepiregulin, ER, ERP.

    Product # :

    CYT-859

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    • sds-page

    Description

    EREG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 69 amino acids (63-108 a.a) and having a molecular mass of 7.7kDa. EREG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    EREG protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE

    sds-page

    EREG-sds-page - Product image 1

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    • Introduction

      Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence.

    • Synonyms

      Epiregulin, Proepiregulin, ER, ERP.

    • 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 MGSVSITKCS SDMNGYCLHG QCIYLVDMSQ NYCRCEVGYT GVRCEHFFL.

    • Background

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

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

      What is the Purity of EREG Protein?
      EREG Protein is >80% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of EREG Protein?
      MGSSHHHHHH SSGLVPRGSH MGSVSITKCS SDMNGYCLHG QCIYLVDMSQ NYCRCEVGYT GVRCEHFFL.

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

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

    Ereg Human His
  • View Data Sheet

    Name :

    POFUT1 Human

    Description:

    Protein O-Fucosyltransferase 1 Human Recombinant

    FUT12, O-Fuc-T, O-FucT-1, O-FUT, GDP-fucose protein O-fucosyltransferase 1, Peptide-O-fucosyltraferase 1,KIAA0180.

    Product # :

    ENZ-679

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    Description

    POFUT1 Human Recombinant produced in E. coli is a single polypeptide chain containing 385 amino acids (27-388) and having a molecular mass of 43.7 kDa. POFUT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The POFUT1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GDP-fucose protein O-fucosyltransferase 1 (POUFUT1), belongs to the glycosyltransferase O-Fuc family. POUFUT1 encodes a member of the glycosyltransferase O-Fuc family and Expressed mainly in pancreas, kidney, lung, heart, brain, liver, placenta and skeletal muscle.POUFUT1 adds O-fucose through an O-glycosidic linkage to Preserve serine or threonine residues in the epidermal growth factor-like repeats of a number of cell surface and emitted proteins. POUFUT1 is involved in ligand-induced receptor signaling. Alternative splicing of this gene results in 2 transcript variants encoding different isoforms.POFUT1 participates in Notch signaling, as Notch ligands can use as POFUT1 substrates.

    • Synonyms

      FUT12, O-Fuc-T, O-FucT-1, O-FUT, GDP-fucose protein O-fucosyltransferase 1, Peptide-O-fucosyltraferase 1,KIAA0180.

    • 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 MGSGSWDPAG YLLYCPCMGR FGNQADHFLG SLAFAKLLNR TLAVPPWIEY QHHKPPFTNL HVSYQKYFKL EPLQAYHRVI SLEDFMEKLA PTHWPPEKRV AYCFEVAAQR SPDKKTCPMK EGNPFGPFWD QFHVSFNKSE LFTGISFSAS YREQWSQRFS PKEHPVLALP GAPAQFPVLE EHRPLQKYMV WSDEMVKTGE AQIHAHLVRP YVGIHLRIGS DWKNACAMLK DGTAGSHFMA SPQCVGYSRS TAAPLTMTMC LPDLKEIQRA VKLWVRSLDA QSVYVATDSE SYVPELQQLF KGKVKVVSLK PEVAQVDLYI LGQADHFIGN CVSSFTAFVK RERDLQGRPS SFFGMDRPPK LRDEF.

    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.

    Pofut1 Human
  • View Data Sheet

    Name :

    Placental Lactogen Sf9, Human

    Description:

    Placental Lactogen Human Recombinant, Sf9

    Chorionic Somatomammotropin Hormone 1, CSH1, Choriomammotropin, Lactogen, CSH2, PL, CSA, CSMT, FLJ75407

    Product # :

    CYT-1164

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    Description

    Placental Lactogen Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 197 amino acids (27-217 aa) and having a molecular mass of 23.1kDa.Placental Lactogen is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The Placental Lactogen solution (0.25mg/ml) contains 30% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Determined by cell proliferation assay using Nb2-11 Rat lymphoma cells. ED50 range for this effect is ≤ 0.8 ng/ml.

    More Info

    • Introduction

      Placental Lactogen is a polypeptide hormone that is produced by the Syncytiotrophoblasts of the Placenta.Placental Lactogen has both GH and Prolactin activities on growth, lactation, and luteal steroid production. In women, placental lactogen secretion begins soon after implantation and increases to 1 g or more a day in late pregnancy. Placental Lactogen Bovine is also capable of activating human and other heterologous GH receptors.

    • Synonyms

      Chorionic Somatomammotropin Hormone 1, CSH1, Choriomammotropin, Lactogen, CSH2, PL, CSA, CSMT, FLJ75407

    • 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

      VQTVPLSRLF DHAMLQAHRA HQLAIDTYQE FEETYIPKDQ KYSFLHDSQT SFCFSDSIPT PSNMEETQQK SNLELLRISL LLIESWLEPV RFLRSMFANN LVYDTSDSDD YHLLKDLEEG IQTLMGRLED GSRRTGQILK QTYSKFDTNS HNHDALLKNY GLLYCFRKDM DKVETFLRMV QCRSVEGSCG FHHHHHH

    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.

    Csh1 Human
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