Search results

1000 results found for “EGF Receptor”

Name

Description

Product #

Price

Quantity

Shipping Method

  • View Data Sheet

    Description:

    TP53RK Binding Protein Human Recombinant

    TP53RK binding protein, PRPK-binding protein, PRPK (p53-related protein kinase)-binding protein, CGI-121.

    Product # :

    PRO-1185

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    TPRKB Human Recombinant produced E. coli is a single polypeptide chain containing 199 amino acids (1-175) and having a molecular mass of 22.2kDa.TPRKB is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TPRKB solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 150mM NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      TPRKB is a member of the CGI121/TPRKB family. TPRKB is localized to nucleus and cytoplasm and is ubiquitously expressed. TPRKB is known to cooperate with TP53RK/PRPK.

    • Synonyms

      TP53RK binding protein, PRPK-binding protein, PRPK (p53-related protein kinase)-binding protein, CGI-121.

    • 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 MGSHMQLTHQ LDLFPECRVT LLLFKDVKNA GDLRRKAMEG TIDGSLINPT VIVDPFQILV AANKAVHLYK LGKMKTRTLS TEIIFNLSPN NNISEALKKF GISANDTSIL IVYIEEGEKQ INQEYLISQV EGHQVSLKNL PEIMNITEVK KIYKLSSQEE SIGTLLDAII CRMSTKDVL

    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.

    Tprkb Human
  • View Data Sheet

    Description:

    Fibroblast Growth Factor-23 Human Recombinant, His Tag

    Tumor-derived hypophosphatemia-inducing factor, HYPF, ADHR, HPDR2, PHPTC, FGF23, FGF-23, Fibroblast Growth Factor-23.

    Product # :

    CYT-374

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    Fibroblast Growth Factor-23 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain expressed with a -6xHis tag containing a total of 257 amino acids (251 a.a. FGF23+ 6 a.a. His tag) and having a molecular mass of 28629.5 Dalton. The FGF-23 is and purified by chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein (0.5mg/ml) was lyophilized from 25mM Tris pH7.5 and 0.6M NaCl solution.

    Purity

    Greater than 90.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Treatment with hrFGF23 has been shown to induce FGFR mediated Erk phosphorylation, reduce plasma PTH levels in rats and to reduce blood phosphate levels.

    More Info

    • Introduction

      FGF-23 is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities and are involved in a variety of biological processes including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF-23 inhibits renal tubular phosphate transport. This gene was identified by its mutations associated with autosomal dominant hypophosphatemic rickets (ADHR), an inherited phosphate wasting disorder. Abnormally high level expression of FGF23 was found in oncogenic hypophosphatemic osteomalacia (OHO), a phenotypically similar disease caused by abnormal phosphate metabolism. Mutations FGF23 have also been shown to cause familial tumoral calcinosis with hyperphosphatemia.

    • Synonyms

      Tumor-derived hypophosphatemia-inducing factor, HYPF, ADHR, HPDR2, PHPTC, FGF23, FGF-23, Fibroblast Growth Factor-23.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Lyophilized Fibroblast Growth Factor 23 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-23 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Fibroblast Growth Factor-23 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MLGARLRLWVCALCSVCSMSVLRAYPNASPLLGSSWGGLIHLYTATARN
      SYHLQIHKNGHVDGAPHQTIYSALMIRSEDAGFVVITGVMSRRYLCMDFR
      GNIFGSHYFDPENCRFQHQTLENGYDVYHSPQYHFLVSLGRAKRAFLPG
      MNPPPYSQFLSRRNEIPLIHFNTPIPRRHTRSAEDDSERDPLNVLKPRAR
      MTPAPASCSQELPSAEDNSPMASDPLGVVRGGRVNTHAGGTGPEGCRP
      FAKFIHHHHHH.

    • Background

      What is the molecular weight/Mw of FGF23 HUMAN, HIS Protein?
      FGF23 HUMAN, HIS Protein has a total Mw of 28.6kDa.

      What is the source or expression system of FGF23 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of FGF23 HUMAN, HIS Protein?
      FGF23 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF23 HUMAN, HIS Protein?
      Treatment with hrFGF23 has been shown to induce FGFR mediated Erk phosphorylation, reduce plasma PTH levels in rats and to reduce blood phosphate levels.

      What is the amino acid sequence of FGF23 HUMAN, HIS Protein?
      MLGARLRLWVCALCSVCSMSVLRAYPNASPLLGSSWGGLIHLYTATARN
      SYHLQIHKNGHVDGAPHQTIYSALMIRSEDAGFVVITGVMSRRYLCMDFR
      GNIFGSHYFDPENCRFQHQTLENGYDVYHSPQYHFLVSLGRAKRAFLPG
      MNPPPYSQFLSRRNEIPLIHFNTPIPRRHTRSAEDDSERDPLNVLKPRAR
      MTPAPASCSQELPSAEDNSPMASDPLGVVRGGRVNTHAGGTGPEGCRP
      FAKFIHHHHHH.

      What applications can FGF23 HUMAN, HIS Protein be used in?
      FGF23 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF23 HUMAN, HIS Protein?
      The endotoxin level is minimal, FGF23 HUMAN, HIS Protein was purified using conventional chromatography techniques.

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

    Fgf23 Human His
  • View Data Sheet

    Description:

    Fibroblast Growth Factor-20 Human Recombinant

    Fibroblast Growth Factor 20, FGF-20, RHDA2, FGF20.

    Product # :

    CYT-875

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    FGF20 Human Recombinant (1-211) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 217 amino acids and having a molecular mass of 24kDa.The FGF-20 is fused to a 6 amino acid His tag [HHHHHH] at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered solution in MOPS, (NH4)2SO4, DTT and EDTA.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as measured in a proliferation assay using mouse NR6R-3T3 cells, is less than 2.5ng/ml.

    More Info

    • Introduction

      Fibroblast growth factor 20 (FGF20) belongs to the FGF gene family and member of FGF-9 subfamily (based upon its structure). Human FGF20 has several receptors which include FGF R1c, FGF R2c, FGF R3b, FGF R3c and FGF R4. FGF20 is expressed a various cells, including dopaminergic neurons, fibroblasts, keratinocytes and breast epithelium, and numerous sites in the fetus.

    • Synonyms

      Fibroblast Growth Factor 20, FGF-20, RHDA2, FGF20.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FGF20 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-20 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 FGF-20 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MHHHHHHAPL AEVGGFLGGL EGLGQQVGSH FLLPPAGERP PLLGERRSAA ERSARGGPGA AQLAHLHGIL RRRQLYCRTG FHLQILPDGS VQGTRQDHSL FGILEFISVA VGLVSIRGVD SGLYLGMNDK GELYGSEKLT SECIFREQFE ENWYNTYSSN IYKHGDTGRR YFVALNKDGT PRDGARSKRH QKFTHFLPRP VDPERVPELY KDLLMYT.

    • Background

      What is the molecular weight/Mw of FGF20 Protein?
      FGF20 Protein has a total Mw of 24kDa.

      What is the source or expression system of FGF20 Protein?
      Escherichia Coli.

      What is the Purity of FGF20 Protein?
      FGF20 Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF20 Protein?
      The ED50, as measured in a proliferation assay using mouse NR6R-3T3 cells, is less than 2.5ng/ml.

      What is the amino acid sequence of FGF20 Protein?
      MHHHHHHAPL AEVGGFLGGL EGLGQQVGSH FLLPPAGERP PLLGERRSAA ERSARGGPGA AQLAHLHGIL RRRQLYCRTG FHLQILPDGS VQGTRQDHSL FGILEFISVA VGLVSIRGVD SGLYLGMNDK GELYGSEKLT SECIFREQFE ENWYNTYSSN IYKHGDTGRR YFVALNKDGT PRDGARSKRH QKFTHFLPRP VDPERVPELY KDLLMYT.

      What applications can FGF20 Protein be used in?
      FGF20 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF20 Protein?
      The endotoxin level is minimal, FGF20 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.

    Fgf20 Human
  • View Data Sheet

    Description:

    Fibroblast Growth Factor-Basic Human Recombinant

    Prostatropin, FGF-basic, fgf2, Basic FGF, HBGF-2, FGF-2, FGF-b.

    Product # :

    CYT-218

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    Fibroblast Growth Factor-2 Human Recombinant (FGF-2) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 154 amino acids and having a molecular mass of 17.2kDa.The FGF-b is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution in 20mM Tris-HCl, pH7.4 and 1M NaCl.

    Purity

    Greater than 98.0% as determined by Analysis by SDS-PAGE.

    Biological Activity

    The ED50, calculated by the dose-dependant proliferation of murine balb/c 3T3 cells is <0.1ng/ml, corresponding to a specific activity of graeter than 1.0x107 Units/mg.

    More Info

    • Introduction

      Basic fibroblast growth factor is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The HPR -binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.

    • Synonyms

      Prostatropin, FGF-basic, fgf2, Basic FGF, HBGF-2, FGF-2, FGF-b.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      AAGSITTLPA LPEDGGSGAF PPGHFKDPKR LYCKNGGFFL RIHPDGRVDG VREKSDPHIK LQLQAEERGV VSIKGVCANR YLAMKEDGRL LASKCVTDEC FFFERLESNN YNTYRSRKYT SWYVALKRTG QYKLGSKTGP GQKAILFLPM SAKS.

    • Background

      FGF 2 HUMAN: Insights into Fibroblast Growth Factor-2

      Basic Fibroblast Growth Factor or FGF 2 HUMAN is a protein with crucial roles in cell growth, tissue repair, and embryonic development. This is part of the larger fibroblast growth factor family and is vital for various biological processes, including the modulation of cell survival activities.

      Production and Properties

      Produced in E. coli, FGF 2 is a non-glycosylated polypeptide chain possessing 154 amino acids with a molecular weight of about 17.2 kDa. It is purified through advanced chromatographic techniques, ensuring high purity and activity for laboratory use.

      Physical Characteristics and Preparation

      The physical form of FGF 2 HUMAN is a sterile, white lyophilized powder. For experimental use, it is reconstituted with sterile water to at least 100µg/ml. This reconstitution is crucial for maintaining the integrity and effectiveness of the protein in various research applications.

      Storage and Handling

      To maintain stability, lyophilized FGF 2 should be stored at -18°C and used within three weeks if kept at room temperature. Once reconstituted, it should be kept at 4°C and used within 2-7 days or stored at -18°C for longer-term storage.

      Proper handling and avoiding repeated freeze-thaw cycles are essential to preserve the protein's functionality.

      Purity and Biological Activity

      FGF 2 is characterized by a purity greater than 98%, verified by SDS-PAGE analysis. Its biological activity is primarily defined by its efficacy in promoting the proliferation of specific cell lines, with an effective dose (ED50) typically below 0.1 ng/ml.

      Research Applications and Impact

      In the research context, FGF 2 is used extensively to study its effects on cell migration, proliferation, and angiogenesis. Moreover, its role in disease models, particularly in cancer and tissue repair studies, makes it a valuable resource for developing new therapeutic approaches.

      Usage Guidelines

      FGF 2 HUMAN is strictly for laboratory research use and is not suitable for drug development, food production, or cosmetic applications. Researchers are advised to comply with safety and handling guidelines to ensure that experiments are conducted under optimal conditions.

      The Broad Impact on Development and Disease

      FGF-2 is known for its multifunctional role across numerous biological processes such as tissue repair, embryonic development, angiogenesis, and even tumorigenesis.

      This growth factor, existing in various synonymous forms such as Basic FGF, FGF-b, and HBGF-2, is essential in cellular processes that underpin both health and disease.

      Furthermore, FGF-2's ability to bind to cellular receptors triggers a cascade of signaling pathways, including PI3K/Akt, MAPK/ERK, and PLCγ, which in turn influence cell growth, migration, and survival.

      These pathways are pivotal in mediating the factor's diverse effects on cell behavior, contributing to its critical roles in wound healing, angiogenesis, and tissue remodeling.

      What is the molecular weight/Mw of FGF 2 Protein?
      FGF 2 Protein has a total Mw of 17.2kDa.

      What is the source or expression system of FGF 2 Protein?
      Escherichia Coli.

      What is the Purity of FGF 2 Protein?
      FGF 2 Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF 2 Protein?
      The ED50, calculated by the dose-dependant proliferation of murine balb/c 3T3 cells is <0.1ng/ml, corresponding to a specific activity of graeter than 1.0x107 Units/mg.

      What is the amino acid sequence of FGF 2 Protein?
      AAGSITTLPA LPEDGGSGAF PPGHFKDPKR LYCKNGGFFL RIHPDGRVDG VREKSDPHIK LQLQAEERGV VSIKGVCANR YLAMKEDGRL LASKCVTDEC FFFERLESNN YNTYRSRKYT SWYVALKRTG QYKLGSKTGP GQKAILFLPM SAKS.

      What applications can FGF 2 Protein be used in?
      FGF 2 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF 2 Protein?
      The endotoxin level is minimal, FGF 2 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.

    Fgf 2 Human
  • View Data Sheet

    Description:

    LIN28 Human Recombinant

    CSDD1, FLJ12457, LIN-28, LIN28A, Protein lin-28 homolog A, ZCCHC1, Zinc finger CCHC domain-containing protein 1, Lin-28A, LIN28.

    Product # :

    PRO-743

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Recombinant Human LIN28 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids (42-209) and having a molecular mass of 21.1 kDa.LIN28 is expressed with a 23 amino acid His tag fused at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LIN28 protein solution (0.5mg/ml) contains 20mM Tris-HCl, pH-8, 10% glycerol, 0.1mM PMSF and 0.1M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE

    More Info

    • Introduction

      LIN28 plays an important role as a 'translational enhancer', leading specific mRNAs to polysomes and therefore increasing the competence of protein synthesis. LIN28 is a marker of undifferentiated human embryonic stem cells and it enhances the efficiency of the formation of induced pluripotent stem (iPS) cells from human fibroblasts. LIN28 binds to the let-7 pre-miRNA and blocks production of the mature let-7 microRNA in mouse embryonic stem cells. Overexpression of LIN28 is associated with human germ-cell tumors.

    • Synonyms

      CSDD1, FLJ12457, LIN-28, LIN28A, Protein lin-28 homolog A, ZCCHC1, Zinc finger CCHC domain-containing protein 1, Lin-28A, LIN28.

    • 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 SSGLVPRGSHRSMGICKWFN VRMGFGFLSM TARAGVALDP PVDVFVHQSK LHMEGFRSLK EGEAVEFTFK KSAKGLESIR VTGPGGVFCI GSERRPKGKS MQKRRSKGDR CYNCGGLDHH AKECKLPPQP KKCHFCQSIS HMVASCPLKA QQGPSAQGKP TYFREEEEEI HSPTLLPEAQ N.

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

    Lin28 Human
  • View Data Sheet

    Description:

    Interleukin-36 Receptor Antagonist Human Recombinant

    Interleukin-36 receptor antagonist protein, FIL1 delta, IL-1-related protein 3, IL-1RP3, Interleukin-1 HY1, IL-1HY1, Interleukin-1 delta, IL-1 delta, Interleukin-1 family member 5, IL-1F5, Interleukin-1 receptor antagonist homolog 1, IL-1ra homolog 1, Interleukin-1-like protein 1, IL-1L1, IL36RN, FIL1D, IL1F5, IL1HY1, IL1L1, IL1RP3, FIL1, PSORP, IL36RA, FIL1(DELTA).

    Product # :

    CYT-009

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    IL1F5 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 155 amino acids and having a molecular mass of 17kDa.The IL1F5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL1F5 was lyophilized after extensive dialysis against 20mM Phosphate buffer, pH7.4.

    Purity

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

    Biological Activity

    As measured by its binding ability in a functional ELISA, immobilized IL1F5 at 1 µg/ml (100 µl/well) can bind rHuIL-1 Rrp2/Fc Chimera with a linear range of 0.15- 5 µg/ml.

    More Info

    • Introduction

      Human interleukin family 1, member 5 (IL-1F5 / FIL1-delta) belongs to the interleukin 1 cytokine family. IL1F5 is expressed by a variety of cells including monocytes, Bcells, dendritic cells/Langerhans cells, keratinocytes,and gastric fundus Parietal and Chief cells. IL1F5 is an antagonist of IL1F9; however IL1F5 activity related to receptor binding remains unclear. Human and mouse IL1F5 share 90% amino acid sequence identity.

    • Synonyms

      Interleukin-36 receptor antagonist protein, FIL1 delta, IL-1-related protein 3, IL-1RP3, Interleukin-1 HY1, IL-1HY1, Interleukin-1 delta, IL-1 delta, Interleukin-1 family member 5, IL-1F5, Interleukin-1 receptor antagonist homolog 1, IL-1ra homolog 1, Interleukin-1-like protein 1, IL-1L1, IL36RN, FIL1D, IL1F5, IL1HY1, IL1L1, IL1RP3, FIL1, PSORP, IL36RA, FIL1(DELTA).

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL1F5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1F5 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 quick spin followed by reconstitution of IL1F5 in PBS to a concentration no less than 100 µg/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 Met-Val-Leu-Ser-Gly.

    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.

    Il1F5 Human
  • View Data Sheet

    Description:

    Interferon Alpha and Beta Receptor Subunit 1 Human Recombinant

    IFN-alpha/beta R1, IFNAR1, AVP, IFN-alpha-REC, IFNAR, IFNBR, IFRC, Interferon alpha/beta receptor 1, IFN-R-1, IFN-alpha/beta receptor 1, Cytokine receptor class-II member 1, Cytokine receptor family 2 member 1, CRF2-1, Type I interferon receptor 1.

    Product # :

    CYT-1138

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info
    • SDS-PAGE

    Description

    IFNAR1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 415 amino acids (28-436a.a.) and having a molecular mass of 47.9kDa. IFNAR1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    IFNAR1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    SDS-PAGE

    More Info

    • Introduction

      Interferon Alpha And Beta Receptor or IFNAR1, is part of the class II cytokine receptor family. IFNAR1 forms one of the two chains of a receptor for interferons alpha and beta. IFNAR1 binds and activates the receptor that stimulates Janus protein kinases, which then phosphorylate few proteins, including STAT1 & STAT2. Furthermore, IFNAR1 also acts as an antiviral factor.

    • Synonyms

      IFN-alpha/beta R1, IFNAR1, AVP, IFN-alpha-REC, IFNAR, IFNBR, IFRC, Interferon alpha/beta receptor 1, IFN-R-1, IFN-alpha/beta receptor 1, Cytokine receptor class-II member 1, Cytokine receptor family 2 member 1, CRF2-1, Type I interferon receptor 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

      KNLKSPQKVE VDIIDDNFIL RWNRSDESVG NVTFSFDYQK TGMDNWIKLS GCQNITSTKC NFSSLKLNVY EEIKLRIRAE KENTSSWYEV DSFTPFRKAQ IGPPEVHLEA EDKAIVIHIS PGTKDSVMWA LDGLSFTYSL VIWKNSSGVE ERIENIYSRH KIYKLSPETT YCLKVKAALL TSWKIGVYSP VHCIKTTVEN ELPPPENIEV SVQNQNYVLK WDYTYANMTF QVQWLHAFLK RNPGNHLYKW KQIPDCENVK TTQCVFPQNV FQKGIYLLRV QASDGNNTSF WSEEIKFDTE IQAFLLPPVF NIRSLSDSFH IYIGAPKQSG NTPVIQDYPL IYEIIFWENT SNAERKIIEK KTDVTVPNLK PLTVYCVKAR AHTMDEKLNK SSVFSDAVCE KTKPGNTSKH HHHHH.

    • Background

      What is the molecular weight/Mw of IFNAR1 HUMAN Protein?
      IFNAR1 HUMAN Protein has a total Mw of 47.9kDa.

      What is the source or expression system of IFNAR1 HUMAN Protein?
      Sf9, Insect cells.

      What is the Purity of IFNAR1 HUMAN Protein?
      IFNAR1 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IFNAR1 HUMAN Protein?
      The biological functionality of IFNAR1 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of IFNAR1 HUMAN Protein?
      KNLKSPQKVE VDIIDDNFIL RWNRSDESVG NVTFSFDYQK TGMDNWIKLS GCQNITSTKC NFSSLKLNVY EEIKLRIRAE KENTSSWYEV DSFTPFRKAQ IGPPEVHLEA EDKAIVIHIS PGTKDSVMWA LDGLSFTYSL VIWKNSSGVE ERIENIYSRH KIYKLSPETT YCLKVKAALL TSWKIGVYSP VHCIKTTVEN ELPPPENIEV SVQNQNYVLK WDYTYANMTF QVQWLHAFLK RNPGNHLYKW KQIPDCENVK TTQCVFPQNV FQKGIYLLRV QASDGNNTSF WSEEIKFDTE IQAFLLPPVF NIRSLSDSFH IYIGAPKQSG NTPVIQDYPL IYEIIFWENT SNAERKIIEK KTDVTVPNLK PLTVYCVKAR AHTMDEKLNK SSVFSDAVCE KTKPGNTSKH HHHHH.

      What applications can IFNAR1 HUMAN Protein be used in?
      IFNAR1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IFNAR1 HUMAN Protein?
      The endotoxin level is minimal, IFNAR1 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.

    Ifnar1 Human
  • View Data Sheet

    Description:

    Interleukin-7 Receptor Human Recombinant

    IL7R, Interleukin 7 Receptor, IL-7 Receptor Subunit Alpha, IL-7R Subunit Alpha,CD127 Antigen, IL-7R-Alpha, CDW127, Interleukin-7 Receptor Subunit Alpha, Interleukin 7 Receptor Isoform H5-6, Interleukin 7 Receptor Alpha Chain, IL-7RA,CD127, IL7RA, ILRA.   

    Product # :

    CYT-1046

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    IL7R produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 461 amino acids (21-239a.a.) and having a molecular mass of 52.5kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). IL7R is expressed with an 242 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL7R protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Interleukin-7 receptor (IL7R) ,is a hematopoietin receptor superfamily member. IL7R takes a vital part in lymphocyte differentiation, proliferation, multiple sclerosis, as well as survival. IL7R protein signaling is vital for T-cell development and regulation of native and memory T-cell homeostasis. Likewise, IL7R is critically needed for the proper function & development of lymphoid cells.

    • Synonyms

      IL7R, Interleukin 7 Receptor, IL-7 Receptor Subunit Alpha, IL-7R Subunit Alpha,CD127 Antigen, IL-7R-Alpha, CDW127, Interleukin-7 Receptor Subunit Alpha, Interleukin 7 Receptor Isoform H5-6, Interleukin 7 Receptor Alpha Chain, IL-7RA,CD127, IL7RA, ILRA.


    • 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

      ADLESGYAQN GDLEDAELDD YSFSCYSQLE VNGSQHSLTC AFEDPDVNIT NLEFEICGAL VEVKCLNFRK LQEIYFIETK KFLLIGKSNI CVKVGEKSLT CKKIDLTTIV KPEAPFDLSV VYREGANDFV VTFNTSHLQK KYVKVLMHDV AYRQEKDENK WTHVNLSSTK LTLLQRKLQP AAMYEIKVRS IPDHYFKGFW SEWSPSYYFR TPEINNSSGE MDLEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH H

    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.

    Il7R Human
  • View Data Sheet

    Description:

    Galectin-2, BioActive Mouse Recombinant

    Galectin-2, Gal-2, Lgals2, 2200008F12Rik, AI324147.

    Product # :

    CYT-1155

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

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

    Description

    LGALS2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids (1-130 a.a) and having a molecular mass of 17.3kDa.LGALS2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    LGALS2 protein (1mg/ml) contains 10% glycerol, 0.1M NaCl, 1mM DTT and 20mM Tris-HCl buffer (pH 8.0).

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Measured by its ability to agglutinate human red blood cells. The ED50 is ≥ 20ug/ml.

    More Info

    • Introduction

      Galectin-2 or LGALS2 is a protein, part of the galectin proteins family. The galectin proteins family holds galectin proteins family lectins that mediates adhesion between cells or cells to ECM. This family also take part in pre-mRNA splicing, apoptosis & tumor progression. Galectin-2 induces apoptosis in T cells that are activated & binds to lymphotoxin-a, also can implicatate on myocardial infarction. LGALS2 from human and mouse share about 65% amino acid sequence resemblance.

    • Synonyms

      Galectin-2, Gal-2, Lgals2, 2200008F12Rik, AI324147.

    • 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 MGSMSEKFEV KDLNMKPGMS LKIKGKIHND VDRFLINLGQ GKETLNLHFN PRFDESTIVC NTSEGGRWGQ EQRENHMCFS PGSEVKITIT FQDKDFKVTL PDGHQLTFPN RLGHNQLHYL SMGGLQISSF KLE

    • Background

      What is the molecular weight/Mw of LGALS2 MOUSE, ACTIVE Protein?
      LGALS2 MOUSE, ACTIVE Protein has a total Mw of 17.3kDa.

      What is the source or expression system of LGALS2 MOUSE, ACTIVE Protein?
      Escherichia Coli.

      What is the Purity of LGALS2 MOUSE, ACTIVE Protein?
      LGALS2 MOUSE, ACTIVE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of LGALS2 MOUSE, ACTIVE Protein?
      Measured by its ability to agglutinate human red blood cells. The ED50 is ≥ 20ug/ml.

      What is the amino acid sequence of LGALS2 MOUSE, ACTIVE Protein?
      MGSSHHHHHH SSGLVPRGSH MGSMSEKFEV KDLNMKPGMS LKIKGKIHND VDRFLINLGQ GKETLNLHFN PRFDESTIVC NTSEGGRWGQ EQRENHMCFS PGSEVKITIT FQDKDFKVTL PDGHQLTFPN RLGHNQLHYL SMGGLQISSF KLE.

      What applications can LGALS2 MOUSE, ACTIVE Protein be used in?
      LGALS2 MOUSE, ACTIVE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for LGALS2 MOUSE, ACTIVE Protein?
      The endotoxin level is minimal, LGALS2 MOUSE, ACTIVE 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.

    Galectin 2 Mouse
  • View Data Sheet

    Description:

    Transcription Elongation Factor A (SII)-Like 8 Human Recombinant

    Transcription elongation factor A protein-like 8, TCEA-like protein 8, Transcription elongation factor S-II protein-like 8, TCEAL8.

    Product # :

    PRO-1188

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    TCEAL8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 125 amino acids (1-117 a.a) and having a molecular mass of 14.7kDa (Molecular weight on SDS-PAGE will appear higher).TCEAL8 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    TCEAL8 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer, pH8.0, 20% glycerol, 1mM DTT and 200mM NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Transcription elongation factor A protein-like 8 (TCEAL8) is a member of the TFS-II family and TFA subfamily. TCEAL8 is involved in transcriptional regulation and localized in nucleus. TFS-II family members contain TFA domains and act as nuclear phosphoproteins which control transcription in a promoter context-dependent mode. Numerous family members are found on the X chromosome.

    • Synonyms

      Transcription elongation factor A protein-like 8, TCEA-like protein 8, Transcription elongation factor S-II protein-like 8, TCEAL8.

    • 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

      MQKSCEENEG KPQNMPKAEE DRPLEDVPQE AEGNPQPSEE GVSQEAEGNP RGGPNQPGQG FKEDTPVRHL DPEEMIRGVD ELERLREEIR RVRNKFVMMH WKQRHSRSRP YPVCFRPLEH 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.

    Tceal8 Human
  • View Data Sheet

    Description:

    Chromosome 19 Open Reading Frame 80 Mouse Recombinant

    Betatrophin, Angiopoietin-like protein 8, Lipasin, Refeeding-induced fat and liver protein, Gm6484, Angptl8, Rifl, EG624219.

    Product # :

    PRO-1576

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    C19ORF80 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 16-198) containing 193 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 21.8kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    C19ORF80 filtered (0.4 µm) and lyophilized from 0.5mg/ml in 30mM acetate buffer, pH-4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Chromosome 19 Open Reading Frame 80 (C19ORF80) is a significant new regulator of lipid metabolism which regulates serum triglyceride levels, possibly by promoting ANGPTL3 cleavage. C19ORF80 belongs to the ANGPTL protein family. C19ORF80 is a hormone which specifically promotes pancreatic beta cell proliferation and beta cell mass expansion, thus improving glucose tolerance. C19ORF80 is mainly expressed in the liver; it is also expressed in adipose tissues. C19ORF80 is expressed in response to food intake and stimulated by insulin.

    • Synonyms

      Betatrophin, Angiopoietin-like protein 8, Lipasin, Refeeding-induced fat and liver protein, Gm6484, Angptl8, Rifl, EG624219.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. C19ORF80 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASVRPAPVAPLG GPEPAQYEEL TLLFHGALQL GQALNGVYRA TEARLTEAGH SLGLYDRALE FLGTEVRQGQ DATQELRTSL SEIQVEEDAL HLRAEATARS LGEVARAQQA LRDTVRRLQV QLRGAWLGQA HQEFETLKAR ADKQSHLLWA LTGHVQRQQR EMAEQQQWLR QIQQRLHTAA LPA.

    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.

    C19Orf80 Mouse
  • View Data Sheet

    Description:

    Neuropilin 1 Human Recombinant

    Neuropilin-1 isoform a, NRP1, BDCA4, CD304, NP1, NRP, VEGF165R, Vascular endothelial cell growth factor 165 receptor.

    Product # :

    CYT-1059

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    NRP1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 843 amino acids (22-856a.a.) and having a molecular mass of 94.8kDa. (Molecular size on SDS-PAGE will appear at approximately 100-150kDa).NRP1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    NRP1 protein solution (0.25mg/ml) contains phosphate buffered saline (pH7.4) and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NRP1 is a coreceptor bound on membranes to tyrosine kinase receptors for semaphorin family proteins and endothelial growth factors, it is a type one transmembrane protein. Neuropilin-1 takes part in cell survival, angiogenesis, invasion, migration, and axon guidance. the protein is a potential target for cancer therapies as it interacts with VEGF (co-receptor).

    • Synonyms

      Neuropilin-1 isoform a, NRP1, BDCA4, CD304, NP1, NRP, VEGF165R, Vascular endothelial cell growth factor 165 receptor.

    • 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

      FRNDKCGDTI KIESPGYLTS PGYPHSYHPS EKCEWLIQAP DPYQRIMINF NPHFDLEDRD CKYDYVEVFD GENENGHFRG KFCGKIAPPP VVSSGPFLFI KFVSDYETHG AGFSIRYEIF KRGPECSQNY TTPSGVIKSP GFPEKYPNSL ECTYIVFAPK MSEIILEFES FDLEPDSNPP
      GGMFCRYDRL EIWDGFPDVG PHIGRYCGQK TPGRIRSSSG ILSMVFYTDS AIAKEGFSAN YSVLQSSVSE DFKCMEALGM ESGEIHSDQI TASSQYSTNW SAERSRLNYP ENGWTPGEDS YREWIQVDLG LLRFVTAVGT QGAISKETKK KYYVKTYKID VSSNGEDWIT IKEGNKPVLF
      QGNTNPTDVV VAVFPKPLIT RFVRIKPATW ETGISMRFEV YGCKITDYPC SGMLGMVSGL ISDSQITSSN QGDRNWMPEN IRLVTSRSGW ALPPAPHSYI NEWLQIDLGE EKIVRGIIIQ GGKHRENKVF MRKFKIGYSN NGSDWKMIMD DSKRKAKSFE GNNNYDTPEL RTFPALSTRF
      IRIYPERATH GGLGLRMELL GCEVEAPTAG PTTPNGNLVD ECDDDQANCH SGTGDDFQLT GGTTVLATEK PTVIDSTIQS EFPTYGFNCE FGWGSHKTFC HWEHDNHVQL KWSVLTSKTG PIQDHTGDGN FIYSQADENQ KGKVARLVSP VVYSQNSAHC MTFWYHMSGS HVGTLRVKLR
      YQKPEEYDQL VWMAIGHQGD HWKEGRVLLH KSLKLYQVIF EGEIGKGNLG GIAVDDISIN NHISQEDCAK PADLDKKNPE IKIDETGSTP GYEGEGEGDK NISRKPGNVL KTLDPLEHHH HHH.

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

    Nrp1 Human
  • View Data Sheet

    Description:

    Epithelial Cell Adhesion Molecule Human Recombinant, Sf9

    Epithelial Cell Adhesion Molecule , Tumor-Associated Calcium Signal Transducer 1, Major Gastrointestinal Tumor-Associated Protein GA733-2, Adenocarcinoma-Associated Antigen, Cell Surface Glycoprotein Trop-1, Epithelial Glycoprotein 314, TACSTD1, EGP314, MIC18, TROP1, M4S1, KSA, Membrane Component, Chromosome 4, Surface Marker (35kD Glycoprotein), Antigen Identified By Monoclonal Antibody AUA1, Human Epithelial Glycoprotein-2, Epithelial Cell Surface Antigen, Epithelial Glycoprotein, KS 1/4 Antigen, CD326 Antigen, GA733-2, HEGP314, HNPCC8, Ep-CAM, DIAR5, EGP-2, EGP40, KS1/4, MK-1, M1S2, ESA, EGP, EPCAM.

    Product # :

    PRO-2238

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    EPCAM produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (24-265 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 248 amino acids and having a molecular mass of 28.2kDa.EPCAM shows multiple bands between 28-40kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      EPCAM is a carcinoma-associated antigen and belongs to a family which includes at least 2 type I membrane proteins. The EPCAM protein has a role in embryonic stem cells proliferation and differentiation. EPCAM is used as a target for immunotherapy treatment of human carcinomas. EPCAM is expressed on most normal epithelial cells and gastrointestinal carcinomas and acts as a homotypic calcium-independent cell adhesion molecule. Epithelial cell adhesion molecules (EPCAM) can act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium for supplying immunological barrier as a first line of defense against mucosal infection. EPCAM gene mutations result in congenital tufting enteropathy.

    • Synonyms

      Epithelial Cell Adhesion Molecule , Tumor-Associated Calcium Signal Transducer 1, Major Gastrointestinal Tumor-Associated Protein GA733-2, Adenocarcinoma-Associated Antigen, Cell Surface Glycoprotein Trop-1, Epithelial Glycoprotein 314, TACSTD1, EGP314, MIC18, TROP1, M4S1, KSA, Membrane Component, Chromosome 4, Surface Marker (35kD Glycoprotein), Antigen Identified By Monoclonal Antibody AUA1, Human Epithelial Glycoprotein-2, Epithelial Cell Surface Antigen, Epithelial Glycoprotein, KS 1/4 Antigen, CD326 Antigen, GA733-2, HEGP314, HNPCC8, Ep-CAM, DIAR5, EGP-2, EGP40, KS1/4, MK-1, M1S2, ESA, EGP, EPCAM.

    • 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

      QEECVCENYK LAVNCFVNNN RQCQCTSVGA QNTVICSKLA AKCLVMKAEM NGSKLGRRAK PEGALQNNDG LYDPDCDESG LFKAKQCNGT STCWCVNTAG VRRTDKDTEI TCSERVRTYW IIIELKHKAR EKPYDSKSLR TALQKEITTR YQLDPKFITS ILYENNVITI DLVQNSSQKT QNDVDIADVA YYFEKDVKGE SLFHSKKMDL TVNGEQLDLD PGQTLIYYVD EKAPEFSMQG LKHHHHHH

    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.

    Epcam Human Sf9
  • View Data Sheet

    Description:

    Galectin-1 Mouse Recombinant

    Galectin-1, Gal-1, 14 kDa lectin, Beta-galactoside-binding lectin L-14-I, Galaptin, Lactose-binding lectin 1, Lectin galactoside-binding soluble 1, S-Lac lectin 1, Lgals1, Gbp, L14, Galbp, L-14.5, Lect14, AA410090.

    Product # :

    CYT-186

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info
    • SDS-PAGE

    Description

    LGALS1 mouse Recombinant produced E. coli is a single polypeptide chain containing 159 amino acids (1-135) and having a molecular mass of 17kDa.LGALS1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LGALS1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    SDS-PAGE

    More Info

    • Introduction

      The galectins are a family of beta-galactoside-binding proteins implicated in modulating cell-cell and cell-matrix interactions. Galectin-1 is an autocrine negative growth factor that regulates cell proliferation. Galectin-1 regulates cell apoptosis and cell differentiation. Galectin-1 binds CD45, CD3 and CD4 & inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of lyn kinase. Galectin-1 and its ligands are one of the master regulators of immune responses as T-cell homeostasis and survival, T-cell immune disorders, inflammation and allergies as well as host–pathogen interactions. Galectin-1 expression or overexpression in tumors and/or the tissue surrounding them must be considered as a sign of the malignant tumor progression that is often related to the long-range dissemination of tumoral cells (metastasis), to their dissemination into the surrounding normal tissue, and to tumor immune-escape. Galectin-1 in its oxidized form plays a number of important roles in the regeneration of the central nervous system after injury. The targeted overexpression (or delivery) of Galectin-1 should be considered as a method of choice for the treatment of some kinds of inflammation-related diseases, neurodegenerative pathologies and muscular dystrophies. In contrast, the targeted inhibition of Galectin-1 expression is what should be developed for therapeutic applications against cancer progression. Galectin-1 is thus a promising molecular target for the development of new and original therapeutic tools. There is 88% homology between the human and mouse galectin-1.

    • Synonyms

      Galectin-1, Gal-1, 14 kDa lectin, Beta-galactoside-binding lectin L-14-I, Galaptin, Lactose-binding lectin 1, Lectin galactoside-binding soluble 1, S-Lac lectin 1, Lgals1, Gbp, L14, Galbp, L-14.5, Lect14, AA410090.

    • 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 MGSHMACGLV ASNLNLKPGE CLKVRGEVAS DAKSFVLNLG KDSNNLCLHF NPRFNAHGDA NTIVCNTKED GTWGTEHREP AFPFQPGSIT EVCITFDQAD LTIKLPDGHE FKFPNRLNME AINYMAADGD FKIKCVAFE.

    • Background

      What is the molecular weight/Mw of LGALS1 MOUSE Protein?
      LGALS1 MOUSE Protein has a total Mw of 17kDa.

      What is the source or expression system of LGALS1 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of LGALS1 MOUSE Protein?
      LGALS1 MOUSE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of LGALS1 MOUSE Protein?
      The biological functionality of LGALS1 MOUSE Protein will be determined in the future.

      What is the amino acid sequence of LGALS1 MOUSE Protein?
      MGSSHHHHHH SSGLVPRGSH MGSHMACGLV ASNLNLKPGE CLKVRGEVAS DAKSFVLNLG KDSNNLCLHF NPRFNAHGDA NTIVCNTKED GTWGTEHREP AFPFQPGSIT EVCITFDQAD LTIKLPDGHE FKFPNRLNME AINYMAADGD FKIKCVAFE.

      What applications can LGALS1 MOUSE Protein be used in?
      LGALS1 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for LGALS1 MOUSE Protein?
      The endotoxin level is minimal, LGALS1 MOUSE 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.

    Lgals1 Mouse
  • View Data Sheet

    Description:

    HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5 Human Recombinant

    HERC5, HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5, CEB1, Hect Domain and RLD 5, Cyclin-E-Binding Protein 1, CEBP1, HECT Domain and RCC1-Like Domain-Containing Protein 5, E3 ISG15--Protein Ligase HERC5, Probable E3 Ubiquitin-Protein Ligase HERC5, EC 6.3.2.- , EC 6.3.2.

    Product # :

    ENZ-797

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    HERC5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 367 amino acids (681-1024 a.a.) and having a molecular mass of 43kDa. HERC5 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    HERC5 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5 (HERC5) is a member of the HERC family of ubiquitin ligases, found in a cluster of HERC family genes on chromosome 4. HERC5 is a protein with a HECT domain and 5 RCC1 repeats. The HERC5 protein localizes to the cytoplasm and perinuclear region and serves as an INF-induced E3 protein ligase that mediates ISGylation of protein targets. HERC5 exhibits antiviral activity towards HIV-1, influenza A virus and human papillomavirus. HERC5 is a major E3 ligase for ISG15 conjugation. HERC5 also serves as a positive regulator of innate antiviral response in cells induced by INF. Pro-inflammatory cytokines upregulate HERC5 in endothelial cells. HERC5 is physically connected with polyribosomes, broadly modifies recently synthesized proteins in a cotranslational fashion.

    • Synonyms

      HERC5, HECT and RLD Domain Containing E3 Ubiquitin Protein Ligase 5, CEB1, Hect Domain and RLD 5, Cyclin-E-Binding Protein 1, CEBP1, HECT Domain and RCC1-Like Domain-Containing Protein 5, E3 ISG15--Protein Ligase HERC5, Probable E3 Ubiquitin-Protein Ligase HERC5, EC 6.3.2.- , 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 MGSFDLTVRR NHLIEDVLNQ LSQFENEDLR KELWVSFSGE IGYDLGGVKK EFFYCLFAEM IQPEYGMFMY PEGASCMWFP VKPKFEKKRY FFFGVLCGLS LFNCNVANLP FPLALFKKLL DQMPSLEDLK ELSPDLGKNL QTLLDDEGDN FEEVFYIHFN VHWDRNDTNL IPNGSSITVN QTNKRDYVSK YINYIFNDSV KAVYEEFRRG FYKMCDEDII KLFHPEELKD VIVGNTDYDW KTFEKNARYE PGYNSSHPTI VMFWKAFHKL TLEEKKKFLV FLTGTDRLQM KDLNNMKITF CCPESWNERD PIRALTCFSV LFLPKYSTME TVEEALQEAI NNNRGFG.

    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.

    Herc5 Human
  • View Data Sheet

    Description:

    Mouse Anti Human Natural Cytotoxicity Triggering Receptor 3

    Natural Cytotoxicity Triggering Receptor 3, LY117, 1C7, Lymphocyte Antigen 117, Activating Natural Killer Receptor P30, Natural Killer Cell P30-Related Protein, NK-p30, NKp30, CD337, MALS, Activating NK-A1 Receptor, CD337 Antigen, NKP30.

    Product # :

    ANT-740

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • formulation
    • More Info

    Formulation

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

    More Info

    • Introduction

      Cytotoxicity Triggering Receptor 3 also known as NCR3 is a natural cytotoxicity receptor (NCR) which assists NK cells in the lysis of tumor cells. Moreover, NCR3 interacts with CD3-zeta (CD247), a T-cell receptor. A single nucleotide polymorphism in the 5' untranslated region of NCR3 has been related with mild malaria suceptibility. Three transcript variants encoding various isoforms have been found for this gene.

    • Synonyms

      Natural Cytotoxicity Triggering Receptor 3, LY117, 1C7, Lymphocyte Antigen 117, Activating Natural Killer Receptor P30, Natural Killer Cell P30-Related Protein, NK-p30, NKp30, CD337, MALS, Activating NK-A1 Receptor, CD337 Antigen, NKP30.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human NCR3 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human NCR3 protein 19-138 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      PAT38D9AT.

    • Applications

      NCR3 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.

    • 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

      NCR3 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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

    Ncr3 Antibody
  • View Data Sheet

    Description:

    S100 Calcium Binding Protein A9 Human Recombinant

    Calgranulin B, 60B8AG, CAGB, CFAG, CGLB, L1AG, LIAG, MAC387, MIF, MRP14, NIF, P14, Protein S100-A9, S100 calcium-binding protein A9.

    Product # :

    PRO-814

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    S100A9 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 122 amino acids (1-114 a.a.) and having a molecular mass of 14.3kDa. S100A9 protein is fused to an 8 amino acid His-Tag at C-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    S100A9 Human solution containing 20mM Tris HCl pH-8, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      S100A9 is part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100A9 protein is localized in the cytoplasm and/or nucleus of a wide range of cells, and participates in the regulation of several cellular processes such as cell cycle progression and differentiation. S100 genes include no less than 13 proteins which are localized as a cluster on chromosome 1q21. S100A9 is involved in the inhibition of casein kinase and altered expression of this protein is associated with the disease cystic fibrosis.

    • Synonyms

      Calgranulin B, 60B8AG, CAGB, CFAG, CGLB, L1AG, LIAG, MAC387, MIF, MRP14, NIF, P14, Protein S100-A9, S100 calcium-binding protein A9.

    • 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

      MTCKMSQLER NIETIINTFH QYSVKLGHPD TLNQGEFKEL VRKDLQNFLK KENKNEKVIE HIMEDLDTNA DKQLSFEEFI MLMARLTWAS HEKMHEGDEG PGHHHKPGLG EGTPLEHHHH 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.

    S100A9 Human
  • View Data Sheet

    Description:

    CCAAT/enhancer binding protein C/EBP Gamma Recombinant Human

    CCAAT/enhancer-binding protein gamma, C/EBP gamma, CEBPG, GPE1BP, IG/EBP-1.

    Product # :

    PRO-434

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    CEBP-g Recombinant Human His-Tag fusion protein produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 146 (aa 39-147) and having a molecular mass of 16.5 kDa. The DNA binding domain of CEBP-g was purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein contains 20mM Tris-HCl pH7.5, 0.1M NaCl and 5mM b-Mercaptoethanol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CCAAT/enhancer binding protein(C/EBP) g is a family of transcription factors all contain a highly conserved, basic-leucine zipper domain at the C-terminus that is involved in dimerization and DNA binding. C/EBP family of transcription factors regulates viral and cellular CCAAT/enhancer element-mediated transcription. C/EBP family consist of several related proteins, C/EBP a,b,g,d, that form homodimers and/or form heterodimers with each other. C/EBP proteins contain the bZIP region, which is characterized by two motifs in the C-terminal half of the protein; a basic region involved in DNA binding and a leucine zipper motif involved in dimerization. C/EBP g may cooperate with Fos to bind PRE- enhancer elements.

    • Synonyms

      CCAAT/enhancer-binding protein gamma, C/EBP gamma, CEBPG, GPE1BP, IG/EBP-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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMPGG GGKAVAPSKQ SKKSSPMDRN SDEYRQRRER NNMAVKKSRL KSKQKAQDTL QRVNQLKEEN ERLEAKIKLL TKELSVLKDL FLEHAHNLAD NVQSISTENT TADGDN.

    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.

    Cebpg Human
  • View Data Sheet

    Description:

    Platelet-Derived Growth Factor B Human Recombinant

    Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, SIS, SSV, PDGF2, c-sis, FLJ12858, PDGF-BB, PDGF B-chain, Platelet-derived growth factor beta polypeptide, Becaplermin.

    Product # :

    CYT-492

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    PDGF-B Human Recombinant mature chain produced in E.Coli is a non-glycosylated, polypeptide chain containing 109 amino acids fragment (82-190) and having a molecular mass of 16.75 kDa. The PDGF-B is fused with an amino-terminal hexahistidine tag and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Platelet-Derived Growth Factor-B is supplied in 25mM Na-Acetate pH 4.8, 1mM EDTA and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The term ‘PDGF’ refers to a family of disulphide bond-linked dimeric isoforms that act as autocrine and paracrine growth factors and are produced by a variety of cell types other than platelets.
      They act as potent mitogens for almost all mesenchymally-derived cells. Aberrant expression is involved in certain cancers, fibroproliferative disorders and atherosclerosis. The protein also contributes to wound healing and neural regeneration. There are four members of the PDGF family – PDGF A, PDGF B, PDGF C and PDGF D. Two distinct types of PDGF-A exist – a short form that is soluble and a long form that is retained by the extracellular matrix.

    • Synonyms

      Glioma-derived growth factor, GDGF, Osteosarcoma-derived Growth Factor, ODGF, SIS, SSV, PDGF2, c-sis, FLJ12858, PDGF-BB, PDGF B-chain, Platelet-derived growth factor beta polypeptide, Becaplermin.

    • 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. Please avoid 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.

    Pdgf B Human
  • View Data Sheet

    Description:

    Holo Transferrin Human

    Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.

    Product # :

    PRO-315

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Human Holo Transferrin is a glycoprotein of approximately 77 kDa.

    Source

    Human serum.

    Formulation

    The protein (10mg/ml) was lyophilized from 20mM NH4HC03 solution.
    May contain traces of buffer salts.

    Purity

    Greater than 98.0% as determined by coomassie blue stained SDS-PAGE and Cellulose Acetate electrophoresis.

    More Info

    • Introduction

      Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
      It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
      Human Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Human Transferrin is Critical for long-term cells growth in-vitro. Human Transferrin is used as detoxificant in media by binding contaminating metal ions. Human Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Human Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells.

    • Synonyms

      Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.

    • Physical Appearance

      Sterile Filtered Pink lyophilized (freeze-dried) powder.

    • Stability

      Store the lyophilized Holo Transferrin between 2-8°C, do not freeze. Upon reconstitution Apo Transferrin 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 Holo Transferrin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Human Virus Test

      FDA approved Plasma from each donor has been tested and found negative for antibodies to HIV-1 & 2, HCV, HBsAG, HBc, HBV, HAV, HIV and Syphilis.

    • Iron Content

      The Iron content was estimated by ICP and was found to be 1232 ppm.

    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.

    Holo Transferrin Human
  • View Data Sheet

    Description:

    Vascular Endothelial Growth Factor Human Recombinant, Plant

    Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    Product # :

    CYT-1213

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    Vascular Endothelial Growth Factor Human Recombinant produced in Oryza Sativa has a molecular mass of 19.2kDa. The VEGF is purified by proprietary chromatographic techniques.

    Source

    Rice Grain

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Determined by the dose-dependent stimulation of the proliferation of human umbilical vein endothelial cells (HUVEC) using a concentration range of 10ng/ml, corresponding to a Specific Activity of 100,000IU/mg

    More Info

    • Introduction

      Vascular endothelial growth factor (VEGF) is an important signaling protein involved in vessel formation As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ). VEGF mediates increased vascular permeability, induces vasculogenesis and endothelial cell production, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor. VEGF is located in normal cartilage though only osteoarthritic cartilage expresses the VEGF receptors, NP1, VEGFR1 and VEGFR2. The VEGF level in the culture media from OA chondrocytes was more than 3 folds higher than in media from normal chondrocytes

    • Synonyms

      Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

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

    Vegf Protein
  • View Data Sheet

    Description:

    Erythropoietin-Alpha Fc-Chimera Human Recombinant

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

    Product # :

    CYT-325

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    Erythropoietin-alpha Fc-Chimera Human Recombinant is produced in Chinese hamster ovary (CHO) cells by recombinant DNA technology is a dimeric, glycosilated, polypeptide chain consisting of two mature human EPO molecules linked to the Fc portion of human IgG1. The Fc component contains the CH2 domain, the CH3 domain and hinge region, but not the CH1 domain of IgG1. As a result of glycosylation, the recombinant protein migrates with an apparent molecular mass of 140 kDa in non-reducing SDS-PAGE.

    Source

    Chinese Hamster Ovary Cells(CHO).

    Formulation

    Each mg of lyophilized powder contains 1x PBS pH-7.4.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependent stimulation of human megakaryoblastic leukemia cells is less than 2.0 ng/ml, corresponding to a Specific Activity of 5.0 x 105 IU/mg.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Background

      What is the molecular weight/Mw of EPOETIN Protein?
      EPOETIN Protein has a total Mw of 140kDa.

      What is the source or expression system of EPOETIN Protein?
      Chinese Hamster Ovary Cells(CHO).

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

      What is the Biological Activity of EPOETIN Protein?
      The ED50 as determined by the dose-dependent stimulation of human megakaryoblastic leukemia cells is less than 2.0 ng/ml, corresponding to a Specific Activity of 5.0 x 105 IU/mg.

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

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

    Epo Alpha Human Fc
  • View Data Sheet

    Description:

    Granulocyte Macrophage-Colony Stimulating Factor Rat Recombinant

    CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim.

    Product # :

    CYT-395

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    Granulocyte Macrophage Colony Stimulating Factor Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 128 amino acids and having a molecular mass of 14590.65 Dalton. GM-CSF Rat Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GM-CSF Rat was lyophilized with no additives.

    Purity

    Greater than 96.0% as determined by:
    (a)Analysis by RP-HPLC.
    (b)Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as calculated by the dose-dependent stimulation of the proliferation of murine FDC-P1 cells is less than 0.01ng/ml, corresponding to a specific activity of > 1×108units/mg.

    More Info

    • Introduction

      GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
      GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.

    • Synonyms

      CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MAPTRSPNPV TRPWKHVDAI KEALSLLNDM RALENEKNED VDIISNEFSI

      QRPTCVQTRL KLYKQGLRGN LTKLNGALTM IASHYQTNCP PTPETDCEIE

      VTTFEDFIKN LKGFLFDIPF DCWKPVQK.

    • Background

      What is the molecular weight/Mw of GM-CSF RAT Protein?
      GM-CSF RAT Protein has a total Mw of 14.59kDa.

      What is the source or expression system of GM-CSF RAT Protein?
      Escherichia Coli.

      What is the Purity of GM-CSF RAT Protein?
      GM-CSF RAT Protein is >96% pure as determined by SDS-PAGE.

      What is the Biological Activity of GM-CSF RAT Protein?
      The ED50 as calculated by the dose-dependent stimulation of the proliferation of murine FDC-P1 cells is less than 0.01ng/ml, corresponding to a specific activity of > 1×108units/mg.

      What is the amino acid sequence of GM-CSF RAT Protein?
      MAPTRSPNPV TRPWKHVDAI KEALSLLNDM RALENEKNED VDIISNEFSI
      QRPTCVQTRL KLYKQGLRGN LTKLNGALTM IASHYQTNCP PTPETDCEIE
      VTTFEDFIKN LKGFLFDIPF DCWKPVQK.

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

      What is the endotoxin level for GM-CSF RAT Protein?
      The endotoxin level is minimal, GM-CSF 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.

    Gm Csf Rat
  • View Data Sheet

    Description:

    Fibronectin Leucine Rich Transmembrane Protein 3 Human Recombinant, HEK

    Fibronectin Leucine Rich Transmembrane Protein 3, Fibronectin-Like Domain, Containing Leucine-Rich Transmembrane Protein 3, HH21, Leucine-Rich Repeat, Transmembrane Protein FLRT3, KIAA1469.

    Product # :

    PRO-2805

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

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

    Description

    FLRT3 Human Recombinant is a single, glycosylated, polypeptide chain (29-528 a.a) containing a total of 506 amino acids and having a molecular mass of 57.3 kDa. FLRT3 is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    FLRT3 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    >40%.  Measured by the ability of the immobilized protein to support the adhesion of Neuro-2a neuroblast cells. When cells are added to human FLRT3 coated plates 5 ug/ml.

    More Info

    • Synonyms

      Fibronectin Leucine Rich Transmembrane Protein 3, Fibronectin-Like Domain, Containing Leucine-Rich Transmembrane Protein 3, HH21, Leucine-Rich Repeat, Transmembrane Protein FLRT3, KIAA1469.

    • 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

      KSCPSVCRCD AGFIYCNDRF LTSIPTGIPE DATTLYLQNN QINNAGIPSD LKNLLKVERI YLYHNSLDEF PTNLPKYVKE LHLQENNIRT ITYDSLSKIP YLEELHLDDN SVSAVSIEEG AFRDSNYLRL LFLSRNHLST IPWGLPRTIE ELRLDDNRIS TISSPSLQGL TSLKRLVLDG NLLNNHGLGD KVFFNLVNLT ELSLVRNSLT AAPVNLPGTN LRKLYLQDNH INRVPPNAFS
      YLRQLYRLDM SNNNLSNLPQ GIFDDLDNIT QLILRNNPWY CGCKMKWVRD WLQSLPVKVN VRGLMCQAPE KVRGMAIKDL NAELFDCKDS GIVSTIQITT AIPNTVYPAQ GQWPAPVTKQ PDIKNPKLTK DHQTTGSPSR KTITITVKSV TSDTIHISWK LALPMTALRL SWLKLGHSPA FGSITETIVT GERSEYLVTA LEPDSPYKVC MVPMETSNLY LFDETPVCIE TETAPLRMYN
      PTTTLNREQE KEPYKNPNLP HHHHHH.

    • Background

      Fibronectin leucine-rich transmembrane protein 3, commonly known as FLRT3, stands as a molecular architect in the intricate landscape of neural development. Its roles, initially discovered in the embryonic nervous system, have expanded to encompass various physiological and pathological processes in both the brain and beyond. This research endeavors to unravel the enigma of FLRT3 protein, exploring its structural intricacies, physiological functions, and its far-reaching implications in neurobiology, embryogenesis, and disease. By delving into FLRT3's multifaceted roles, scientists aim to decipher the underlying mechanisms that govern its diverse functions and explore potential therapeutic avenues in the realms of neuroscience and beyond.

      Structural Complexities of FLRT3:

      FLRT3 belongs to the FLRT family, characterized by extracellular leucine-rich repeats (LRRs) and a transmembrane domain. These structural motifs enable FLRT3 to participate in a myriad of interactions, including binding with cell adhesion molecules and guidance cues. Understanding the three-dimensional architecture of FLRT3 is fundamental for unraveling its molecular partnerships, biological activities, and its contributions to cell adhesion and signaling.

      Physiological Functions in Neural Development:

      In the developing nervous system, FLRT3 acts as a guidance molecule, steering growing axons and dendrites to their precise destinations. Through interactions with other cell surface receptors and ligands, FLRT3 modulates axon pathfinding, synapse formation, and neuronal migration. Its presence in growth cones and developing neural circuits underscores its significance in sculpting the intricate neural networks essential for proper brain function.

      Beyond Neural Development:

      Beyond its canonical roles in neurodevelopment, FLRT3 has emerged as a versatile player in various physiological processes. It participates in tissue morphogenesis, modulates cell adhesion, and influences immune responses. Recent studies have also implicated FLRT3 in cancer progression, highlighting its involvement in pathological conditions and making it a potential target for therapeutic interventions in cancer therapy.

      FLRT3 as a Therapeutic Target:

      The diverse roles of FLRT3 in neural development and diseases position it as an attractive target for therapeutic interventions. Modulating FLRT3 interactions offers novel avenues for neurological disorder treatments, including neurodevelopmental disorders and neurodegenerative diseases. Moreover, understanding FLRT3's involvement in cancer biology opens doors for innovative cancer therapies, making it a promising target for precision medicine approaches.

      FLRT3, with its intricate structural features and diverse functional roles, stands as a linchpin in the realms of neuroscience, embryogenesis, and disease. Its multifaceted contributions to neural development, tissue morphogenesis, and disease pathogenesis underscore its significance in both health and pathology. As researchers continue to unravel FLRT3’s complexities, they not only deepen our understanding of fundamental biological processes but also pave the way for groundbreaking discoveries in neuroscience and therapeutic interventions, ultimately shaping the future landscape of medicine and scientific inquiry.

    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.

    Flrt3 Protein