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Search results

1000 results found for “Visinin-Like Protein”

Name

Description

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  • View Data Sheet

    Name :

    DHH Human

    Description:

    Desert Hedgehog Human Recombinant

    HHG-3, Desert Hedgehog homolog, MGC35145, Desert hedgehog protein, DHH.

    Product # :

    CYT-467

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    Description

    DHH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 197 amino acids (23-198) and having a molecular mass of 22 kDa. DHH is fused to His-tag (20 a.a.) at N-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DHH solution containing 20mM MES pH-5.5, 0.5mM DTT and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      DHH is part of the Hedgehog family which encodes signaling molecules that are involved in regulating morphogenesis. DHH protein is a precursor that is autocatalytically cleaved, the N-terminal portion is soluble and contains the signalling activity while the C-terminal portion is involved in precursor processing. Additionally, the C-terminal product covalently attaches a cholesterol moiety to the N-terminal product, restricting the N-terminal product to the cell surface and preventing it from freely diffusing throughout the organism. Defects in DHH protein have been associated with partial gonadal dysgenesis (PGD) accompanied by minifascicular polyneuropathy. DHH plays a role both male gonadal differentiation and perineurial development.
      DHH plays a role in intercellular signaling which is essential for a variety of patterning events during development. DHH functions as a spermatocyte survival factor in the testes & is essential for testes development.

    • Synonyms

      HHG-3, Desert Hedgehog homolog, MGC35145, Desert hedgehog protein, DHH.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MCGPGRGPVG RRRYARKQLV PLLYKQFVPG VPERTLGASG PAEGRVARGS ERFRDLVPNY NPDIIFKDEE NSGADRLMTE RCKERVNALA IAVMNMWPGV RLRVTEGWDE DGHHAQDSLH YEGRALDITT SDRDRNKYGL LARLAVEAGF DWVYYESRNH VHVSVKADNS LAVRAGG.

    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.

    Dhh Human
  • View Data Sheet

    Name :

    COPS7A Human

    Description:

    COP9 Signalosome Subunit 7A Human Recombinant

    COP9 Signalosome Subunit 7A, COPS7A, Dermal Papilla-Derived Protein 10, CSN7A, SGN7a, JAB1-Containing Signalosome Subunit 7a, COP9 Complex Subunit 7a, COP9 Constitutive Photomorphogenic Homolog Subunit 7A, COP9 Signalosome Complex Subunit 7a, DERP10, Signalosome Subunit 7a.

    Product # :

    PRO-1947

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    Description

    COPS7A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 298 amino acids (1-275) and having a molecular mass of 32.7 kDa.COPS7A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The COPS7A solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      COP9 Signalosome Subunit 7A (COPS7A) is a component of the COP9 signalosome complex (CSN), a complex involved in a variety of cellular and developmental processes. The CSN complex is a vital regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, thus leading to decrease in the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. This complex is also involved in phosphorylation of p53/TP53, JUN, I-kappa-B-alpha/NFKBIA, ITPK1 and IRF8/ICSBP, probably through its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN stimulates and protects degradation by the Ubl system, respectively.

    • Synonyms

      COP9 Signalosome Subunit 7A, COPS7A, Dermal Papilla-Derived Protein 10, CSN7A, SGN7a, JAB1-Containing Signalosome Subunit 7a, COP9 Complex Subunit 7a, COP9 Constitutive Photomorphogenic Homolog Subunit 7A, COP9 Signalosome Complex Subunit 7a, DERP10, Signalosome Subunit 7a.

    • 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 MGSMSAEVKV TGQNQEQFLL LAKSAKGAAL ATLIHQVLEA PGVYVFGELL DMPNVRELAE SDFASTFRLL TVFAYGTYAD YLAEARNLPP LTEAQKNKLR HLSVVTLAAK VKCIPYAVLL EALALRNVRQ LEDLVIEAVY ADVLRGSLDQ RNQRLEVDYS IGRDIQRQDL SAIARTLQEW CVGCEVVLSG IEEQVSRANQ HKEQQLGLKQ QIESEVANLK KTIKVTTAAA AAATSQDPEQ HLTELREPAP GTNQRQPSKK ASKGKGLRGS AKIWSKSN.

    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.

    Cops7A Human
  • View Data Sheet

    Name :

    KRT18 Bovine

    Description:

    Cytokeratin-18 Bovine

    Keratin type I cytoskeletal 18, Cytokeratin-18, CK-18, Keratin-18, K18, KRT18,CYK18,Cell proliferation-inducing gene 46 protein.

    Product # :

    PRO-2785

    Price :

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    Description

    KRT18 Bovine having a calculated molecular mass of 45 kDa, pI-5.4.

    Source

    Bovine liver.

    Formulation

    KRT18 was lyophilized from a 1mg/ml solution containing 30mM Tris/HCI pH 8, 9M urea, 2mM EDTA, 2mM DTT and 10mM methylammonium chloride.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Keratin type I cytoskeletal 18, Cytokeratin-18, CK-18, Keratin-18, K18, KRT18,CYK18,Cell proliferation-inducing gene 46 protein.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store the lyophilized KRT18 between 2-8°C, do not freeze. Upon reconstitution KRT18 should be stored at -20°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized KRT18 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Background

      Keratin-18 (K18) is an intermediate filament protein that plays a vital role in maintaining the structural integrity of epithelial cells. Extensive research has been conducted on K18 in human and murine models, shedding light on its functions and implications for various epithelial tissues.

      However, the study of K18 in bovine tissues is an emerging area with potential for advancing our understanding of epithelial cell biology and its applications in veterinary medicine and biotechnology. Bovine tissues, such as the liver and gastrointestinal tract, are of particular interest due to their relevance in cattle production and food safety.

      This research aims to provide a comprehensive exploration of K18 in bovine tissues, elucidating its functions, structural significance, and potential applications.
      The primary objective of this research is to elucidate the role of K18 in bovine tissues, particularly in maintaining the structural integrity of epithelial cells.

      In vitro and ex vivo experiments, utilizing bovine epithelial cell cultures and tissue specimens, will be conducted to investigate how K18 contributes to cellular morphology, cytoskeletal organization, and tissue resilience. Understanding these mechanisms is fundamental for deciphering the complexities of epithelial cell biology in bovine species.
      The second objective is to assess the relevance of bovine K18 in veterinary medicine and cattle production. Studies involving bovine models will be conducted to evaluate the impact of K18 mutations or variations on tissue health, disease susceptibility, and meat quality. These investigations may provide valuable insights into potential applications in cattle breeding and food safety.


      The third objective is to explore the potential biotechnological applications of bovine K18. Research will investigate the use of K18-expressing bovine cells as models for studying epithelial-related diseases and for developing tissue engineering approaches for veterinary medicine and biotechnology.
      By delving into the functions and roles of K18 in bovine tissues, this research aims to expand our knowledge of epithelial cell biology, its implications for veterinary medicine, and its potential applications in biotechnology and cattle production.

    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.

    Keratin 18 Bovine
  • View Data Sheet

    Name :

    FABP7 Human, His

    Description:

    Fatty Acid Binding Protein-7 Human Recombinant, His Tag

    MRG, BLBP, FABPB, B-FABP, DKFZp547J2313, Fatty acid-binding protein brain, Fatty acid-binding protein 7, Brain lipid-binding protein, Mammary-derived growth inhibitor related, FABP7.

    Product # :

    PRO-661

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    Description

    FABP7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids and having a molecular mass of 19.39kDa. FABP7 is fused to His-Tag at N-terminus and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The FABP7 protein solution contains 20mM Tris-HCl pH-8 and 50% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      FABP7 is a brain fatty acid binding protein. Fatty acid binding proteins (FABPs) are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. FABPs are are inovlved in fatty acid uptake, transport, and metabolism. FABP7 is expressed in radial glia by the activation of Notch receptors and binds DHA with the highest affinity among all of FABPs. FABP7 plays an important role in transport of hydrophobic ligand with potential morphogenic activity during cns development. FABP7 is required for the establishment of the radial glial fiber system in developing brain, a system that is necessary for the migration of immature neurons to establish cortical layers (by similarity).

    • Synonyms

      MRG, BLBP, FABPB, B-FABP, DKFZp547J2313, Fatty acid-binding protein brain, Fatty acid-binding protein 7, Brain lipid-binding protein, Mammary-derived growth inhibitor related, FABP7.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    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.

    Fabp7 Human His
  • View Data Sheet

    Name :

    PAIP2 Human

    Description:

    Polyadenylate-Binding Protein-Interacting protein 2 Human Recombinant

    Poly(A) Binding Protein Interacting Protein 2, PABP- interacting protein 2, HSPC218, PAIP-2, PAIP2A, Polyadenylate-binding protein-interacting protein 2, PAIP2, MGC72018.

    Product # :

    PRO-748

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    Description

    Recombinant Human PAIP2 produced in E.Coli is a single,non-glycosylated polypeptide chain containing 147 amino acids (1-127 a.a.) and having a molecular mass of 17.1 kDa.PAIP2 human recombinant is fused to 20 amino acid His Tag at N-terminus and purified by convential chromatogrpahy techniques.

    Source

    Escherichia Coli.

    Formulation

    The PAIP2 protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT & 10% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PAIP2 has a role as a repressor in the regulation of translation initiation of poly(A)-containing mRNAs. PAIP2 inhibitory activity on translation is mediated through its action on PABPC1. PAIP2 displaces the interaction of PABPC1 with poly(A) RNA and competes with PAIP1 for binding to PABPC1. PAIP2 association with PABPC1 results in disruption of the cytoplasmic poly(A) RNP structure organization.

    • Synonyms

      Poly(A) Binding Protein Interacting Protein 2, PABP- interacting protein 2, HSPC218, PAIP-2, PAIP2A, Polyadenylate-binding protein-interacting protein 2, PAIP2, MGC72018.

    • 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 MKDPSRSSTS PSIINEDVII NGHSHEDDNP FAEYMWMENE EEFNRQIEEE LWEEEFIERC FQEMLEEEEE HEWFIPARDL PQTMDQIQDQ FNDLVISDGS SLEDLVVKSN LNPNAKEFVP GVKYGNI.

    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.

    Paip2 Human
  • View Data Sheet

    Name :

    MYL12A Human

    Description:

    Myosin Light Chain 12A Human Recombinant

    Myosin regulatory light chain 12A, MLC-2B, Myosin RLC, Myosin regulatory light chain 2 nonsarcomeric, Myosin regulatory light chain MRLC3, MYL12A, MLCB, MRLC3, RLC, MRCL3, MYL2B.

    Product # :

    PRO-902

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    Description

    MYL12A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 195 amino acids (1-171 a.a.) and having a molecular mass of 22.4kDa.MYL12A is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MYL12A protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Myosin regulatory light chain 12A (MYL12A) has a vital role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. The MYL12A protein is involved in cytokinesis, receptor capping, and cell locomotion.

    • Synonyms

      Myosin regulatory light chain 12A, MLC-2B, Myosin RLC, Myosin regulatory light chain 2 nonsarcomeric, Myosin regulatory light chain MRLC3, MYL12A, MLCB, MRLC3, RLC, MRCL3, MYL2B.

    • 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 MGSHMSSKRT KTKTKKRPQR ATSNVFAMFD QSQIQEFKEA FNMIDQNRDG FIDKEDLHDM LASLGKNPTD EYLDAMMNEA PGPINFTMFL TMFGEKLNGT DPEDVIRNAF ACFDEEATGT IQEDYLRELL TTMGDRFTDE EVDELYREAP IDKKGNFNYI EFTRILKHGA KDKDD.

    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.

    Myl12A Human
  • View Data Sheet

    Name :

    SARS Envelope, His

    Description:

    SARS-Associated Coronavirus Envelope Recombinant, His Tag

    Product # :

    SARS-004

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    • description
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    Description

    The E.coli derived recombinant protein contains the Envelope protein 1-76 amino acids immunodominant regions fused to 6xHis tag at C-terminal.

    Source

    Escherichia Coli.

    Formulation

    SARS Envelope protein solution is supplied in PBS.

    Purity

    Protein is >90% pure as determined SDS-PAGE.

    More Info

    • Introduction

      SARS Associated Coronavirus Envelope is a small membrane protein that takes major part in the life cycle of the virus. This protein is needed for the assembly, budding, creation of the envelope and pathogenesis. This protein contains 3 outer structural proteins, the membrane (M), envelope (E), and spike (S) proteins. Spike (S)-glycoprotein of the virus interacts with a cellular receptor and mediates membrane fusion to assure viral entry thetarget cells. Accordingly, S-protein has a major part in virus infection cycle and is the mainly target of neutralizing antibodies.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Protein is shipped on ice packs. Upon arrival, Store at -20°C.

    • Specificity

      Immunoreactive with sera of SARS-infected individuals.

    • Purification Method

      Purified by proprietary chromatographic technique.

    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.

    product_image.jpg
  • View Data Sheet

    Name :

    PCNP Human

    Description:

    PEST proteolytic Signal Containing Nuclear Protein Human Recombinant

    PEST proteolytic signal-containing nuclear protein, PCNP, PEST-containing nuclear protein.

    Product # :

    PRO-906

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    Description

    PCNP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 202 amino acids (1-178 a.a.) and having a molecular mass of 21.5kDa.PCNP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PCNP protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PEST proteolytic signal containing nuclear protein (PCNP) is a nuclear protein involved in cell cycle regulation and tumorigenesis. The PCNP protein is ubiquitinated post-translationally by NIRF (an ubiquitin ligase). The PCNP exists as 3 isoforms produced by alternative splicing events.

    • Synonyms

      PEST proteolytic signal-containing nuclear protein, PCNP, PEST-containing nuclear protein.

    • 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 MGSHMADGKA GDEKPEKSQR AGAAGGPEEE AEKPVKTKTV SSSNGGESSS RSAEKRSAEE EAADLPTKPT KISKFGFAIG SQTTKKASAI SIKLGSSKPK ETVPTLAPKT LSVAAAFNED EDSEPEEMPP EAKMRMKNIG RDTPTSAGPN SFNKGKHGFS DNQKLWERNI KSHLGNVHDQ DN.

    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.

    Pcnp Human
  • View Data Sheet

    Name :

    RNF181 Human

    Description:

    Ring Finger Protein 181 Human Recombinant

    Ring Finger Protein 181, E3 Ubiquitin-Protein Ligase RNF181, HSPC238, EC 6.3.2.-.

    Product # :

    PRO-1218

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    Description

    RNF181 Human Recombinant produced in E. coli is a single polypeptide chain containing 176 amino acids (1-153) and having a molecular mass of 20.3 kDa.RNF181 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The RNF181 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      E3 ubiquitin-protein ligase RNF181 (RNF181) accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the thioester form and subsequently directly transfers the ubiquitin to targeted substrates. RNF181 is widely expressed, with the highest levels in the liver and heart and the lowest levels in the brain and skeletal muscle. RNF181 is also expressed in platelets (at protein level).

    • Synonyms

      Ring Finger Protein 181, E3 Ubiquitin-Protein Ligase RNF181, HSPC238, EC 6.3.2.-.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMASYFDE HDCEPSDPEQ ETRTNMLLEL ARSLFNRMDF EDLGLVVDWD HHLPPPAAKT VVENLPRTVI RGSQAELKCP VCLLEFEEEE TAIEMPCHHL FHSSCILPWL SKTNSCPLCR YELPTDDDTY EEHRRDKARK QQQQHRLENL HGAMYT.

    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.

    Rnf181 Human
  • View Data Sheet

    Name :

    MRPL28 Human

    Description:

    Mitochondrial Ribosomal Protein L28 Human Recombinant

    MAAT1, p15, 39S ribosomal protein L28, mitochondrial, L28mt, MRP-L28, Melanoma-associated antigen recognized by T-lymphocytes.

    Product # :

    PRO-1279

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    Description

    MRPL28 Human Recombinant produced in E. coli is a single polypeptide chain containing 222 amino acids (56-256) and having a molecular mass of 25.8 kDa. MRPL28 is fused to 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The MRPL28 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.5), 0.1M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      MRPL28 is found in a variety of normal tissues such as spleen, testis, thymus, liver, kidney, brain, adrenal, lung and retinal tissue. 39S ribosomal protein L28, mitochondrial (MRPL28), is a part of the ribosomal protein L28P family. Mammalian mitochondrial ribosomal proteins encoded by nuclear genes and helps in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. MRPL28 is an important therapeutic reagent for HLA-A24 (A24) patients since this antigen is distinguished by tumor-infiltrating lymphocyte (TIL) 1290, which targets the A24 serotype.

    • Synonyms

      MAAT1, p15, 39S ribosomal protein L28, mitochondrial, L28mt, MRP-L28, Melanoma-associated antigen recognized by T-lymphocytes.

    • 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 MNGQRERVED VPIPIYFPPE SQRGLWGGEG WILGQIYANN DKLSKRLKKV WKPQLFEREF YSEILDKKFT VTVTMRTLDL IDEAYGLDFY ILKTPKEDLC SKFGMDLKRG MLLRLARQDP QLHPEDPERR AAIYDKYKEF AIPEEEAEWV GLTLEEAIEK QRLLEEKDPV PLFKIYVAEL IQQLQQQALS EPAVVQKRAS GQ.

    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.

    Mrpl28 Human
  • View Data Sheet

    Name :

    LTF Human

    Description:

    Lactoferrin Human (Breast Milk)

    Lactotransferrin, Lactoferrin, Growth-inhibiting protein 12, Talalactoferrin, LTF, GIG12, LF, HLF2, Neutrophil Lactoferrin.

    Product # :

    PRO-1590

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    Description

    The Human Lactoferrin produced from Human breast milk has a molecular mass of 76.165kDa (calculated without glycosylation) containing 691 amino acid residues.

    Source

    Human breast milk.

    Formulation

    LTF protein filtered (0.4µm) and lyophilized in 0.5 mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lactoferrin is a glycoprotein that belongs to the transferrin family of iron binding proteins. It is found in human breast milk as well as most epithelial surface secretions including tears, nasogastric, saliva, and bronchial. Lactoferrin binds 2 molecules of iron with very high affinity. Lactoferrin inhibits bacterial growth by withholding iron, its N-terminal region is an antimicrobial peptide. Lactotransferrin acts synergistically with lysozyme to potentiate the activity of both proteins. The multifunctional protein lactoferrin has many physiological possible roles. It is often referred to as an innate defense protein and frequently serves as the first line of defense in protection against pathogens. It has been shown to have the ability to bind iron, it is a natural anti-bacterial, anti-fungal and anti-viral, it is an antioxidant and it also has immunomodulatory properties. It has many beneficial properties, which make it a good candidate for a number of product applications. Considerable research is currently going on to explain the various suggested biological functions of lactoferrin.

    • Synonyms

      Lactotransferrin, Lactoferrin, Growth-inhibiting protein 12, Talalactoferrin, LTF, GIG12, LF, HLF2, Neutrophil Lactoferrin.

    • 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 0.5 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

      GRRRSVQWCA VSQPEATKCF QWQRNMRKVR GPPVSCIKRD SPIQCIQAIA ENRADAVTLD GGFIYEAGLA PYKLRPVAAE VYGTERQPRT HYYAVAVVKK GGSFQLNELQ GLKSCHTGLR RTAGWNVPIG TLRPFLNWTG PPEPIEAAVA RFFSASCVPG ADKGQFPNLC RLCAGTGENK CAFSSQEPYF SYSGAFKCLR DGAGDVAFIR ESTVFEDLSD EAERDEYELL CPDNTRKPVD KFKDCHLARV PSHAVVARSV NGKEDAIWNL LRQAQEKFGK DKSPKFQLFG SPSGQKDLLF KDSAIGFSRV PPRIDSGLYL GSGYFTAIQN LRKSEEEVAA RRARVVWCAV GEQELRKCNQ WSGLSEGSVT CSSASTTEDC IALVLKGEAD AMSLDGGYVY TAGKCGLVPV LAENYKSQQS SDPDPNCVDR PVEGYLAVAV VRRSDTSLTW NSVKGKKSCH TAVDRTAGWN IPMGLLFNQT GSCKFDEYFS QSCAPGSDPR SNLCALCIGD EQGENKCVPN SNERYYGYTG AFRCLAENAG DVAFVKDVTV LQNTDGNNNE AWAKDLKLAD FALLCLDGKR KPVTEARSCH LAMAPNHAVV SRMDKVERLK QVLLHQQAKF GRNGSDCPDK FCLFQSETKN LLFNDNTECL ARLHGKTTYE KYLGPQYVAG ITNLKKCSTS PLLEACEFLR K.

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

    Ltf Human
  • View Data Sheet

    Name :

    GAGA-POZ

    Description:

    GAGA-POZ Drosophila Melanogaster Recombinant

    Transcription factor GAGA, Trithorax-like protein, GAGA factor, GAF, Adh transcription factor 2, Neural conserved at 70F, Trl, Adf-2, GAGA, Nc70F, TFGAGA, CG33261, GAGA-POZ.

    Product # :

    PRO-435

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    Description

    GAGA-POZ Drosophila Melanogaster Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids & having a molecular mass of 14 kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein containing 10mM HEPES (pH-7.4) and 25mM NaCl.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      The GAGA factor is a sequence-specific DNA-binding protein, which participates in the regulation of the expression of a variety of different classes of genes in Drosophila such as many developmentally regulated genes, stress induced genes, and cell cycle regulated genes, as well as housekeeping genes. GAGA contains a C-terminal glutamine-rich domain and a highly conserved N-terminal POZ domain which reported to be involved in self-oligomerization in a number of other POZ domain containing proteins. In case of GAGA protein, the N-terminal POZ domain mediates the formation of oligomers both in vitro and in vivo.

    • Synonyms

      Transcription factor GAGA, Trithorax-like protein, GAGA factor, GAF, Adh transcription factor 2, Neural conserved at 70F, Trl, Adf-2, GAGA, Nc70F, TFGAGA, CG33261, GAGA-POZ.

    • 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

      MSLPMNSLYS LTWGDYGTSL VSAIQLLRCH GDLVDCTLAA GGRSFPAHKI VLCAASPFLLDLLKNTPCKH PVVMLAGVNA NDLEALLEFV YRGEVSVDHA QLPSLLQAAQ CLNIQGLAPQTVTKDDYTTH.

    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.

    Gaga Factor
  • View Data Sheet

    Name :

    Follistatin Human

    Description:

    Follistatin Human Recombinant

    FST, FS

    Product # :

    CYT-232

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    Description

    Follistatin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 288 amino acids and having a total molecular mass of 31.5kDa.The FST is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution containing no additives.

    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 the ability to neutralize ACTV inhibitory effect of mouse MPC-11 cells. The expected ED50 is 100-400ng/ml, corresponding to a Specific Activity of 2,500-10,000units/mg in the presence of 7.5ng/ml ACTV A.

    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 functions as an ACTV antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).

    • Synonyms

      FST, FS

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Follistatin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FST 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 Follistatin 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 Gly-Asn-Cys-Trp-Leu.

    • Background

      What is the molecular weight/Mw of FOLLISTATIN HUMAN Protein?
      FOLLISTATIN HUMAN Protein has a total Mw of 31.5kDa.

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

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

      What is the Biological Activity of FOLLISTATIN HUMAN Protein?
      The activity is determined by the ability to neutralize ACTV inhibitory effect of mouse MPC-11 cells. The expected ED50 is 100-400ng/ml, corresponding to a Specific Activity of 2,500-10,000units/mg in the presence of 7.5ng/ml ACTV A.

      What is the amino acid sequence of FOLLISTATIN HUMAN Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Asn-Cys-Trp-Leu.

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

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

    Follistatin 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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    • More Info
    • 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.

    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.

    Bdnf Human
  • View Data Sheet

    Name :

    ICOS Human

    Description:

    Inducible T Cell Costimulator 4 Human Recombinant

    Inducible T Cell Costimulator, Activation-Inducible Lymphocyte Immunomediatory Molecule, Inducible T-Cell Costimulator, AILIM, Inducible T-Cell Co-Stimulator, Inducible Costimulator, CD278 Antigen, CD278, CVID1.   

    Product # :

    PRO-2534

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    Description

    ICOS produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 362 amino acids (21-140a.a.) and having a molecular mass of 40.8kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). ICOS is expressed with an 242 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ICOS protein solution (0.25mg/ml) contains 20mM MES buffer (pH 5.5), 40% glycerol, 2mM DTT and 1mM EDTA 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ICOS (inducible T-cell costimulatory) belongs to the CD28 family of immune-assisted stimulatory receptors. ICOS forms homodimers and takes a significant part in immune responses, cell-cell signaling, as well as regulation of cell proliferation. The interaction of B7-H2 / ICOS takes a vital role in T-cell differentiation, T-B cell interaction in addition to humoral immune response is essential for the formation of reproductive centers as well as the production of cytokine IL-4. Moreover, ICOS is more effective in inducing IL-10 production, a cytokine which is important for the inhibitory function of T regulatory cells. The ICOS-B7RP-1 and B7-1 / B7-2-CD28 / CTLA-4 pathways offer a significant second signal which can regulate the inhibition, activation and fine regulation of T-lymphocyte responses. ICOS stimulates the production of Th1 and Th2 cytokines, however it can also participate in the generation of Th2 cells.

    • Synonyms

      Inducible T Cell Costimulator, Activation-Inducible Lymphocyte Immunomediatory Molecule, Inducible T-Cell Costimulator, AILIM, Inducible T-Cell Co-Stimulator, Inducible Costimulator, CD278 Antigen, CD278, CVID1.

    • 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

      ADPEINGSAN YEMFIFHNGG VQILCKYPDI VQQFKMQLLK GGQILCDLTK TKGSGNTVSI KSLKFCHSQL SNNSVSFFLY NLDHSHANYY FCNLSIFDPP PFKVTLTGGY LHIYESQLCC QLKLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH
      HH

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

    Icos Human
  • View Data Sheet

    Name :

    Collagen-III Bovine

    Description:

    Bovine Collagen-III

    Product # :

    PRO-2731

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    Description

    Mouse Collagen-III is a natural protein purified from washed dissected tissue into dilute acetic acid. Collagen-I is purified by proprietary chromatographic techniques.

    Source

    Bovine washed dissected tissue.

    Formulation

    Collagen-III was lyophilized without additives.

    Purity

    > 90.0%.

    More Info

    • Introduction

      Collagen, a major component of the extracellular matrix, is a fibrous protein that provides tensile strength to tissues giving them structural integrity. Collagen and its derivative, gelatin, have been widely used in medical, pharmaceutical and consumer products for more than 100 years. The supply of these materials, created from animal remains, is both abundant and inexpensive. However, most formulations are not highly purified and have the potential to cause an inflammatory reaction in some product users. In addition, concerns have been raised over the last several years about the potential for contamination of bovine products with the agent that causes mad cow disease and its human variant, Creutzfeldt-Jakob Disease. Animal collagens are subject to extensive modifications that continue over the life of the molecule in the extracellular space. These differences influence both the extractability of collagens from tissue and the biophysical characteristics of these collagens. As a result, collagens isolated from tissues exhibit significant lot-to-lot variability and, as bulk materials, are often analytically intractable. Products that contain animal-derived collagen can induce potentially harmful inflammatory or immune responses in humans and pose risk of contamination with viruses or prions, potentially life-threatening pathogens. Recombinant collagens are essentially identical to the native collagen protein thereby reducing the risk of inflammation, immune response, and disease as compared to animal-sourced collagen.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Collagen-III although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution Collagen-III should be stored at 4C between 2-7 days and for future use below -18C.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 add 20 mM acetic acid to prepare a working stock solution of 1-5 mg/ml, which can then be further diluted to other aqueous solutions. Suspension should be shaken or stirred for several hours or overnight between 2-8°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.

    Collagen Iii Bovine
  • View Data Sheet

    Name :

    ctxB

    Description:

    Cholera Toxin B subunit Recombinant

    Cholera enterotoxin subunit B, Cholera enterotoxin B chain, Cholera enterotoxin gamma chain, Choleragenoid, ctxB, toxB.

    Product # :

    PRO-2605

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    Description

    Cholera Toxin B subunit Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 103 amino acids and having a molecular mass of 11.6kDa.ctxB is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ctxB is supplied as a 0.2 μm filtered solution conteining 5mM PB, pH 7.0, 75mM NaCl, and 50 % glycerol.

    Purity

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

    More Info

    • Introduction

      Cholera Toxin B subunit (ctxB) Cholera is a protein complex secreted by the bacterium Vibrio cholerae. ctxB is responsible for the massive, watery diarrhea characteristic of cholera infection. The cholera toxin is an oligomeric complex made up of 6 protein subunits: a single copy of the A subunit and5 copies of the B subunit, denoted as AB5. Subunit B binds while subunit A activates the G protein which activates adenylate cyclase. The five B subunits form a five-membered ring. The A subunit has 2 important segments. The A1 portion of the chain (CTA1) is a globular enzyme payload that ADP-ribosylates G proteins, while the A2 chain (CTA2) forms an extended alpha helix which sits snugly in the central pore of the B subunit ring.

    • Synonyms

      Cholera enterotoxin subunit B, Cholera enterotoxin B chain, Cholera enterotoxin gamma chain, Choleragenoid, ctxB, toxB.

    • 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

      TPQNITDLCA EYHNTQIYTL NDKIFSYTES LAGKREMAII TFKNGAIFQV EVPGSQHIDS QKKAIERMKD TLRIAYLTEA KVEKLCVWNN KTPHAIAAIS MAN.

    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.

    Ctxb Protein
  • View Data Sheet

    Name :

    EGF Rat Protein

    Description:

    Epidermal Growth Factor Rat

    Urogastrone, URG, EGF.

    Product # :

    CYT-556

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    Description

    Epidermal Growth Factor Rat purified from submandibular gland is a single, glycosylated, polypeptide chain having a molecular mass of 6.15 kDa.The EGF is purified by proprietary chromatographic techniques.

    Source

    Adult Male Rat Submandibular Glands.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution containing 0.01M sodium acetate buffer.

    Purity

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

    More Info

    • Introduction

      Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide.
      EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.

    • Synonyms

      Urogastrone, URG, EGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Background

      Illuminating Epidermal Growth Factor Rat Recombinant: Deciphering Cellular Signaling and Therapeutic Potential

      Abstract:

      This research paper delves into the enigmatic realm of Epidermal Growth Factor Rat Recombinant (EGF-RR), unraveling its intricate molecular attributes, signaling cascades, and therapeutic prospects. By employing cutting-edge methodologies encompassing protein expression, receptor binding assays, and bioinformatics analyses, this study sheds light on the multifaceted interplay between EGF-RR and cellular responses, offering novel avenues for therapeutic interventions.

      Introduction:

      Epidermal Growth Factor (EGF) is pivotal in cellular regulation. This paper navigates the complexities of Epidermal Growth Factor Rat Recombinant (EGF-RR), focusing on its unique molecular properties and potential therapeutic applications.

      Protein Expression and Purification:

      The study embarks on precise gene optimization to enhance EGF-RR expression. Purification techniques like affinity chromatography yield purified EGF-RR, primed for subsequent analyses.

      Receptor Binding Assays and Ligand Interaction:

      Employing advanced receptor binding assays, the paper deciphers EGF-RR's engagement with its cognate receptor. Quantitative assessments uncover binding kinetics, shedding light on the intricacies of EGF-RR's molecular interaction.

      Cellular Signaling Pathways and Responses:

      In vitro cellular assays unveil the signaling cascades ignited by EGF-RR. Through quantitative phosphoproteomic profiling, the study unravels phosphorylation events triggered by EGF-RR, delineating its role in cellular proliferation, migration, and differentiation.

      Bioinformatics Insights and Structural Modeling:

      Bioinformatics tools facilitate molecular dynamics simulations, offering insights into EGF-RR's receptor interactions and downstream signaling pathways. Structural modeling captures EGF-RR's conformational changes during signaling cascades.

      Therapeutic Implications and Future Prospects:

      EGF-RR's intricate signaling dynamics open avenues for therapeutic exploration. Harnessing its potential in wound healing, tissue regeneration, and cancer modulation emerges as a promising avenue for precision medicine.

      Challenges and Future Directions:

      Challenges, including context-specific responses, beckon further investigation. Future research should delve into cross-talk between signaling pathways and EGF-RR's contributions to diverse disease contexts.

      Conclusion:

      A fusion of advanced methodologies and visionary insights unveils Epidermal Growth Factor Rat Recombinant as an intriguing subject. Its molecular intricacies and complex cellular interplay ignite prospects for therapeutic breakthroughs, ushering in a new era of precision medicine.

      What is the molecular weight/Mw of EGF RAT Protein?
      EGF RAT Protein has a total Mw of 6.15kDa.

      What is the source or expression system of EGF RAT Protein?
      Adult Male Rat Submandibular Glands.

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

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

      What is the amino acid sequence of EGF RAT Protein?
      EGF RAT Protein is composed from 53 amino acids.

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

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

    Egf Rat
  • View Data Sheet

    Name :

    BLOC1S2 Human

    Description:

    Biogenesis of Lysosomal Organelles Complex-1, Subunit 2 Human Recombinant

    Biogenesis of lysosomal organelles complex-1 subunit 2, BLOS2, BLOC-1 subunit 2, Centrosome-associated protein, centrosome protein oncogene, centrosomal 10 kDa protein, RP11-316M21.4, CEAP, FLJ30135, MGC10120.

    Product # :

    PRO-1094

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    Description

    BLOC1S2 Human Recombinant produced in E. coli is a single polypeptide chain containing 166 amino acids (1-142) and having a molecular mass of 18.5kDa.BLOC1S2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The BLOC1S2 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 50mM NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      BLOC1S2 is a member of the BLOC1S2 family. Biogenesis of lysosome-related organelles complex 1 or BLOC-1 is a universally expressed multisubunit protein complex which is essential for regular biogenesis of specialized organelles of the endosomal-lysosomal system, like melanosomes and platelet dense granules. BLOC1S2 takes part in cell proliferation.

    • Synonyms

      Biogenesis of lysosomal organelles complex-1 subunit 2, BLOS2, BLOC-1 subunit 2, Centrosome-associated protein, centrosome protein oncogene, centrosomal 10 kDa protein, RP11-316M21.4, CEAP, FLJ30135, MGC10120.

    • 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 MGSHMAAAAE GVLATRSDEP ARDDAAVETA EEAKEPAEAD ITELCRDMFS KMATYLTGEL TATSEDYKLL ENMNKLTSLK YLEMKDIAIN ISRNLKDLNQ KYAGLQPYLD QINVIEEQVA ALEQAAYKLD AYSKKLEAKY KKLEKR

    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.

    Bloc1S2 Human
  • View Data Sheet

    Name :

    Adiponectin Human, HEK

    Description:

    Adiponectin Human Recombinant, HEK

    Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    Product # :

    CYT-434

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    • sds-page

    Description

    Acrp30 Human Recombinant produced in HEK cells is a glycosylated polypeptide chain containing 234 amino acids (19-244a.a.) and having a molecular mass of 25.5kDa. Acrp30 is expressed with a FLAG tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    HEK293 (Human Embryonic Kidney cell line).

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5mg/ml in 50mM phosphate Buffer, 75mM NaCl, pH 7.4.

    Purity

    Greater than 98% as determined by HPLC and SDS PAGE.

    Biological Activity

    In vitro gluconeogenesis assay in primary hepatocytes was performed, showing the Adiponectin human derived from mammalian cells can inhibit glucose production. The ED50 was ~6 µg/ml.

    sds-page

    adiponectin human HEK sds-page - Product image 1

    More Info

    • Introduction

      Adiponectin is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.

    • Synonyms

      Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      For long term, store lyophilized AdipoQ 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. The lyophilized protein remains stable for 24 months when stored at -20°C.

    • Solubility

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

    • Amino Acid Sequence

      ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDDDDK.

    • Background

      What is the molecular weight/Mw of adiponectin Protein?
      Adiponectin Protein has a total Mw of 25.5kDa.

      What is the source or expression system of adiponectin Protein?
      HEK293.

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

      What is the Biological Activity of adiponectin Protein?
      In vitro gluconeogenesis assay in primary hepatocytes was performed, showing the Adiponectin human derived from mammalian cells can inhibit glucose production. The ED50 was ~6 µg/ml.

      What is the amino acid sequence of adiponectin Protein?
      ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDDDDK.

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

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

    Adiponectin Human Hek
  • View Data Sheet

    Name :

    PfHSP70

    Description:

    Plasmodium Falciparum HSP70 Recombinant

    Product # :

    MAL-001

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    Description

    The E.Coli derived recombinant Plasmodium falciparum contains the Plasmodium falciparum HSP70 protein epitopes 33-114 amino acids.

    Formulation

    150mM Imidazole, pH 8.0, 150mM NaCl, 150mM Sodium Phosphate and 50% glycerol.

    Purity

    Protein is >95% pure as determined by 10% PAGE (coomassie staining) and RP-HPLC.

    More Info

    • Introduction

      Plasmodium falciparum heat shock proteins (PfHSPs) contribute to immunopathological alterations in infected hosts PfHSP70s may have a significant function during parasite adaptation in its environments. They have also been a focus of considerable attention due to their immunodominant antigenic nature and their properties as mediators of protective immunity.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      PfHSP70 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      Use as an antigen in ELISA and Western Blots.

    • Purification Method

      Purified by proprietary chromatographic technique

    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.

    Pfhsp70
  • View Data Sheet

    Name :

    EFNA3 Human

    Description:

    Ephrin A3 Human Recombinant

    Ephrin-A3, EFL2, Ehk1-L, EPLG3, LERK3, EPH-related receptor tyrosine kinase ligand 3.

    Product # :

    PRO-1460

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    Description

    EFNA3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids (23-214 a.a) and having a molecular mass of 24kDa. EFNA3 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    EFNA3 protein solution (1mg/ml) containing 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

      EFNA3 belongs to the ephrin (EPH) family. The ephrins and EPH-related receptors include thelargest subfamily of receptor protein-tyrosine kinases which have been implicated in mediating developmental events, especially in the nervous system and in erythropoiesis. Ephrins are divided into the ephrin-A (EFNA) class and the ephrin-B (EFNB) class, based on their structures and sequence relationships. The Ephrins from the EFNA class are anchored to the membrane by aglycosylphosphatidylinositol linkage, while the others from the EFNB class are transmembrane proteins.

    • Synonyms

      Ephrin-A3, EFL2, Ehk1-L, EPLG3, LERK3, EPH-related receptor tyrosine kinase ligand 3.

    • 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 MGSHMQGPGG ALGNRHAVYW NSSNQHLRRE GYTVQVNVND YLDIYCPHYN SSGVGPGAGP GPGGGAEQYV LYMVSRNGYR TCNASQGFKR WECNRPHAPH SPIKFSEKFQ RYSAFSLGYE FHAGHEYYYI STPTHNLHWK CLRMKVFVCC ASTSHSGEKP VPTLPQFTMG PNVKINVLED FEGENPQVPK LEKSISG

    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.

    Efna3 Human
  • View Data Sheet

    Name :

    FABP3 Human, Native

    Description:

    Fatty Acid Binding Protein-3 Human, Native

    Fatty acid-binding protein heart, H-FABP, Heart-type fatty acid-binding protein, Muscle fatty acid-binding protein, M-FABP, Mammary-derived growth inhibitor, MDGI, FABP3, FABP11, O-FABP.

    Product # :

    PRO-2794

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    • More Info

    Description

    FABP3 Human produced in Human cardiac muscle tissue having a molecular mass of 15kDa and is purified by proprietary chromatographic technique.

    Source

    Human heart tissue.

    Formulation

    FABP3 was lyophilized from 10mM Tris-HCl, pH 8.0.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Fatty acid-binding protein heart, H-FABP, Heart-type fatty acid-binding protein, Muscle fatty acid-binding protein, M-FABP, Mammary-derived growth inhibitor, MDGI, FABP3, FABP11, O-FABP.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Fatty Acid Binding Protein-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FABP3 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 FABP3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Background

      FABP3 is abundantly expressed in cardiac and skeletal muscle tissues, where it serves as a crucial mediator in the cellular handling of fatty acids. By facilitating the uptake, transport, and utilization of fatty acids, FABP3 ensures a steady supply of energy, making it indispensable for the high-energy-demanding heart and skeletal muscles. Beyond its role in energy metabolism, FABP3 has been implicated in diverse cellular processes, including inflammation, oxidative stress response, and cellular differentiation.

      Molecular Insights:

      At the molecular level, FABP3 exhibits a remarkable affinity for long-chain fatty acids. Its unique binding properties enable it to shuttle fatty acids to specific cellular compartments, such as mitochondria, for β-oxidation. Additionally, FABP3 is intricately involved in the regulation of gene expression, modulating the activity of various transcription factors and signaling pathways. Understanding these molecular intricacies is key to deciphering FABP3's diverse functions.

      Physiological Significance:

      In cardiac muscle, FABP3 plays a crucial role in myocardial energy metabolism. During periods of increased energy demand, such as cardiac stress or exercise, FABP3 ensures a rapid supply of fatty acids for ATP production. Its absence or dysfunction has been associated with impaired cardiac function and increased susceptibility to ischemic injury. In skeletal muscles, FABP3 contributes to the utilization of fatty acids as an energy source during sustained physical activity.

      Implications in Disease:

      Research indicates that alterations in FABP3 expression and function are linked to several pathological conditions. In cardiovascular diseases, FABP3 has emerged as a potential biomarker for myocardial infarction, reflecting myocardial damage. Moreover, studies have highlighted its involvement in insulin resistance, diabetes, and metabolic syndrome, emphasizing its significance in metabolic disorders.

      Therapeutic Prospects:

      The unique properties of FABP3 have garnered attention in drug development. Researchers are exploring FABP3-targeted therapies for cardiovascular diseases and metabolic disorders. Modulating FABP3 activity presents a promising avenue for managing conditions characterized by dysregulated fatty acid metabolism and oxidative stress.

      Conclusion:

      FABP3, the unassuming intracellular fatty acid chaperone, plays a central role in human physiology and disease. Its intricate involvement in energy metabolism, cellular signaling, and disease pathogenesis underscores its significance as a research subject. As our understanding of FABP3 deepens, it opens doors to innovative diagnostic approaches and therapeutic interventions, potentially impacting millions of lives worldwide.

    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.

    Fabp 3 Human
  • View Data Sheet

    Name :

    TBCA Human

    Description:

    Tubulin Folding Cofactor A Human Recombinant

    Tubulin-specific chaperone A, Tubulin-folding cofactor A, CFA, TCP1-chaperonin cofactor A, TBCA.

    Product # :

    PRO-705

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    TBCA Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 108 amino acids (1-108 a.a.) and having a molecular mass of 12.8 kDa.The TBCA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TBCA solution contains 20mM Tris-HCl buffer pH 7.5, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TBCA is a tubulin-folding protein which is involved in the early step of the tubulin folding pathway. TBCA is one of four proteins (cofactors A, D, E, and C) implicated in the pathway directing to properly folded beta-tubulin from folding intermediates. Cofactors A and D are thought to be a factor in capturing and stabilizing beta-tubulin in a quasi-native confirmation. TBCA is crucial for cell viability, if reduced it causes a decrease in the amount of soluble tubulin, alterations in microtubules and G1 cell cycle arrest. Cofactor E attaches to the cofactor D-tubulin complex, afterward, interaction with cofactor C triggers the release of tubulin polypeptides that are committed to the native state.

    • Synonyms

      Tubulin-specific chaperone A, Tubulin-folding cofactor A, CFA, TCP1-chaperonin cofactor A, TBCA.

    • 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

      MADPRVRQIK IKTGVVKRLV KEKVMYEKEA KQQEEKIEKM RAEDGENYDI KKQAEILQES RMMIPDCQRR LEAAYLDLQR ILENEKDLEE AEEYKEARLV LDSVKLEA.

    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.

    Tbca Human
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