Search results
1000 results found for “Collagen”
Name
Description
Product #
Price
Quantity
Shipping Method
- View Data Sheet
Name :
GALE HumanDescription:
UDP-Galactose-4-Epimerase Human Recombinant
UDP-glucose 4-epimerase, EC=5.1.3.2, Galactowaldenase, UDP-galactose 4 epimerase, GALE, SDR1E1, FLJ95174, FLJ97302.
Product # :
ENZ-537Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
GALE Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 368 amino acids (1-348 a.a.) and having a molecular mass of 40.4 kDa. The GALE is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GALE Human solution containing 20mM Tris pH-8, 5mM DTT, 0.1M NaCl, 1mM EDTA & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
GALE is an enzyme that participates as the third enzyme in the Leloir pathway of galactose metabolism. GALE is a homodimeric epimerase localized in bacterial, plant, and mammalian cells. GALE inhances the reverse chemical reaction, the conversion of UDP-glucose to UDP-galactose. UDP-galactose builds galactose-containing proteins and fats, which have a crucial part in chemical signaling, building cellular structures, transporting molecules, and producing energy.
-
Synonyms
UDP-glucose 4-epimerase, EC=5.1.3.2, Galactowaldenase, UDP-galactose 4 epimerase, GALE, SDR1E1, FLJ95174, FLJ97302.
-
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 MAEKVLVTGG AGYIGSHTVL ELLEAGYLPV VIDNFHNAFR GGGSLPESLR RVQELTGRSV EFEEMDILDQ GALQRLFKKY SFMAVIHFAG LKAVGESVQK PLDYYRVNLT GTIQLLEIMK AHGVKNLVFS SSATVYGNPQ YLPLDEAHPT GGCTNPYGKS KFFIEEMIRD LCQADKTWNA VLLRYFNPTG AHASGCIGED PQGIPNNLMP YVSQVAIGRR EALNVFGNDY DTEDGTGVRD YIHVVDLAKG HIAALRKLKE QCGCRIYNLG TGTGYSVLQM VQAMEKASGK KIPYKVVARR EGDVAACYAN PSLAQEELGW TAALGLDRMC EDLWRWQKQN PSGFGTQA.
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.
- View Data Sheet
Name :
CLEC4E HumanDescription:
C-type Lectin Domain Family 4, Member E Human Recombinant
C-Type Lectin Domain Family 4, Member E, MINCLE, C-Type (Calcium Dependent, Carbohydrate-Recognition Domain) Lectin, Superfamily Member 9, Macrophage-Inducible C-Type Lectin, C-Type Lectin Superfamily Member 9, CLECSF9, C-Type Lectin Domain Family 4 Member E, C-type lectin domain family 4 member E.
Product # :
PRO-2189Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CLEC4E Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids (41-219 a.a) and having a molecular mass of 22.9kDa. CLEC4E is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CLEC4E protein solution (0.25mg/ml) containing 20mM Tris 8.0 and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
C-type lectin domain family 4, member E, also known as CLEC4E is a C-type lectin receptor expressed through a wide range of antigens which presents cells including macrophages, neutrophils, dendritic cells as well as B cells; Furthermore, a variety of stimuli including stress are acknowledged to induce the expression of CLEC4E.
-
Synonyms
C-Type Lectin Domain Family 4, Member E, MINCLE, C-Type (Calcium Dependent, Carbohydrate-Recognition Domain) Lectin, Superfamily Member 9, Macrophage-Inducible C-Type Lectin, C-Type Lectin Superfamily Member 9, CLECSF9, C-Type Lectin Domain Family 4 Member E, C-type lectin domain family 4 member E.
-
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 MRCVVTFRIF QTCDEKKFQL PENFTELSCY NYGSGSVKNC CPLNWEYFQS SCYFFSTDTI SWALSLKNCS AMGAHLVVIN SQEEQEFLSY KKPKMREFFI GLSDQVVEGQ WQWVDGTPLT KSLSFWDVGE PNNIATLEDC ATMRDSSNPR QNWNDVTCFL NYFRICEMVG INPLNKGKSL.
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.
- View Data Sheet
Name :
F8 HumanDescription:
Coagulation Factor-VIII Human
Coagulation factor VIII, Procoagulant component, Antihemophilic factor, AHF, F8, F8C, F8B, HEMA, FVIII, DXS1253E, F8 protein.
Product # :
PRO-317Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- biological activity
- More Info
Description
Human Factor VIII produced from Human Plasma contains 2332 amino acids and having a molecular mass of 330kDa. Factor-VIII is effective in the correction and prevention of severe bleeding episodes attributed to Factor VIII deficiency. The Factor-VIII is purified by proprietary chromatographic techniques.
Source
Human Plasma.
Formulation
The lyophilized protein 200IU/ml was lyophilized from a sterile solution containing 1.5% Glycine, 160mM Calcium chloride and 25mM NaCitrate and 25mM NaCl.
Biological Activity
The potency was found to be 10 Units/mg.
More Info
-
Introduction
Coagulation factor VIII participates in the intrinsic pathway of blood coagulation; factor VIII is a cofactor for factor IXa which, in the presence of Ca+2 and phospholipids, converts factor X to the activated form Xa. This gene produces two alternatively spliced transcripts. Transcript variant 1 encodes a large glycoprotein, isoform a, which circulates in plasma and associates with von Willebrand factor in a noncovalent complex. This protein undergoes multiple cleavage events. Transcript variant 2 encodes a putative small protein, isoform b, which consists primarily of the phospholipid binding domain of factor VIIIc. This binding domain is essential for coagulant activity. Defects in this gene results in hemophilia A, a common recessive X-linked coagulation disorder.
-
Synonyms
Coagulation factor VIII, Procoagulant component, Antihemophilic factor, AHF, F8, F8C, F8B, HEMA, FVIII, DXS1253E, F8 protein.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Factor-VIII although stable at room temperature for 1 week, should be stored desiccated between 2-8°C. Upon reconstitution Factor-VIII should be stored at 4°C.
-
Solubility
It is recommended to reconstitute the lyophilized Factor-VIII in sterile 18MΩ-cm H2O at a concentration of 200IU/ml, which can then be further diluted to other aqueous solutions.
Make sure that the vial has reached room temperature prior to its reconstitution, otherwise it might precipitate.
-
Human Virus Test
The plasma is collected from donors with Hepatitis B vaccinated. Each unit of plasma has been tested for HBsAg, Anti-HIV-1/2 plus O and Anti-HCV by using the imported kits which are approved by Federal Drug Administration (FDA).
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.
- View Data Sheet
Name :
ASS1 AntibodyDescription:
Argininosuccinate Synthase 1, Mouse Anti Human
ASS, CTLN1, EC 6.3.4.5, ASS1, Argininosuccinate Synthase 1.
Product # :
ANT-639Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
-
Introduction
ASS1 is involved in the urea cycle, which is a sequence of chemical reactions that is localized in liver cells. The urea cycle processes excess nitrogen that is generated as the body uses proteins. The surplus nitrogen is used to create a molecule called urea, which is excreted from the body in urine.
-
Synonyms
ASS, CTLN1, EC 6.3.4.5, ASS1, Argininosuccinate Synthase 1.
-
Physical Appearance
Sterile filtered colorless solution.
-
Immunogen
Anti-human ASS1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human ASS1 amino acids 1-412 purified from E. coli.
-
Ig Subclass
Mouse IgG2a heavy chain and k light chain.
-
Clone
PAT1G11AT.
-
Applications
ASS1 antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF 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
ASS1 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.
- View Data Sheet
Name :
CDKN1B AntibodyDescription:
Cyclin-Dependent Kinase Inhibitor 1B, Mouse Anti Human
Cyclin-dependent kinase inhibitor 1B, Cyclin-dependent kinase inhibitor p27, p27Kip1, CDKN1B, KIP1, MEN4, CDKN4, MEN1B.
Product # :
ANT-640Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
-
Introduction
Cyclin-dependent kinase inhibitor 1B (CDKN1B) is a member of the Cip/Kip family of cyclin dependent kinase (Cdk) inhibitor proteins. The CDKN1B protein binds to and prevents the activation of cyclin E-CDK2 or cyclin D-CDK4 complexes, and so controls the cell cycle progression at G1. CDKN1B is often referred to as a cell cycle inhibitor protein since its major function is to stop or slow down the cell division cycle. The degradation of the CDKN1B protein, which is triggered by its CDK dependent phosphorylation and ensuing ubiquitination by SCF complexes, is compulsory for the cellular transition from inactive to the proliferative state.
-
Synonyms
Cyclin-dependent kinase inhibitor 1B, Cyclin-dependent kinase inhibitor p27, p27Kip1, CDKN1B, KIP1, MEN4, CDKN4, MEN1B.
-
Physical Appearance
Sterile filtered colorless solution.
-
Immunogen
Anti-human CDKN1B mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human CDKN1B amino acids 1-198 purified from E. coli.
-
Ig Subclass
Mouse IgG1 heavy chain and k light chain.
-
Clone
PAT7B9AT.
-
Applications
CDKN1B antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF 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
CDKN1B 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.
- View Data Sheet
Name :
TGFB1 (113 a.a.) HumanDescription:
Transforming Growth Factor-Beta 1 (113 a.a.) Human Recombinant
Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1.
Product # :
CYT-679Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
TGF-b 1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 113 amino acids (279-390 a.a.) and having a total molecular mass of 12.9 kDa. TGF-b 1 (113 a.a.) is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TGF-b 1 solution contains 10mM Sodium Citrate (pH3.5) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Transforming growth factor betas (TGFBetas) mediate many cell-cell interactions that occur during embryonic development. Three TGFBetas have been identified in mammals. TGFBeta1, TGFBeta2 and TGFBeta3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
-
Synonyms
Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 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
MALDTNYCFS STEKNCCVRQ LYIDFRKDLG WKWIHEPKGY HANFCLGPCP YIWSLDTQYS KVLALYNQHN PGASAAPCCV PQALEPLPIVYYVGRKPKVE QLSNMIVRSC KCS.
-
Background
Title: Transforming Growth Factor-Beta 1 (113 a.a.) Human Recombinant: A Key Regulator of Cellular Processes with Therapeutic Potential
Abstract:
Transforming Growth Factor-Beta 1 (TGF-β1) is a multifunctional cytokine that plays a crucial role in various cellular processes, including cell growth, differentiation, and immune modulation. The development of TGF-β1 human recombinant proteins has provided valuable tools for studying its biological functions and therapeutic applications. This research paper explores the production process, characteristics, and potential therapeutic uses of TGF-β1 human recombinant, highlighting its importance and clinical significance.Introduction:
TGF-β1 is a pivotal cytokine involved in numerous physiological and pathological processes, such as embryonic development, tissue repair, and immune regulation. Harnessing the therapeutic potential of TGF-β1 has been facilitated by the development of TGF-β1 human recombinant proteins using recombinant DNA technology. These recombinant proteins have become valuable tools for investigating the biological functions of TGF-β1 and exploring its therapeutic applications.Production Process and Characteristics:
TGF-β1 human recombinant proteins are produced using recombinant DNA technology, allowing for the expression of the TGF-β1 gene in different host systems. The resulting recombinant proteins possess similar structural and functional characteristics to native TGF-β1. They exhibit the ability to bind to the TGF-β receptor, initiate intracellular signaling pathways, and modulate various cellular responses.Therapeutic Applications:
TGF-β1 human recombinant proteins have shown promise in a wide range of therapeutic applications. They have been investigated for their potential in tissue regeneration and wound healing, as TGF-β1 plays a crucial role in promoting cell proliferation and extracellular matrix production. Additionally, TGF-β1 has been studied in the context of fibrotic diseases, such as pulmonary fibrosis and liver fibrosis, where it is implicated in the fibrotic cascade. Furthermore, TGF-β1 has been explored as a potential target for antitumor therapies due to its involvement in tumor progression and immune evasion.Advantages and Challenges:
The use of TGF-β1 human recombinant proteins offers several advantages, including the ability to study and manipulate its biological functions in a controlled manner. Recombinant proteins also provide a consistent and reproducible source of TGF-β1, overcoming the challenges associated with sourcing native TGF-β1 from biological samples. However, challenges remain in optimizing production processes, ensuring correct protein folding, and maintaining protein stability.Conclusion:
TGF-β1 human recombinant proteins have emerged as valuable tools for studying the biological functions of TGF-β1 and exploring its therapeutic applications. The production of TGF-β1 recombinant proteins using recombinant DNA technology allows for the investigation of its diverse roles in cellular processes. The therapeutic potential of TGF-β1 human recombinant proteins extends to tissue regeneration, fibrotic diseases, and cancer research. Continued research and development efforts are essential to further optimize production processes, address challenges, and fully exploit the clinical benefits of TGF-β1 human recombinant proteins.
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.
- View Data Sheet
Name :
Thymosin β4Description:
Thymosin-b4 Human Recombinant
Thymosin beta-4, T beta 4, Fx , TB4X, PTMB4, TMSB4.
Product # :
HOR-003Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Thymosin b4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 43 amino acids and having a molecular mass of 4.9kDa.The Thymosin b4 Human is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2um filtered concentrated solution in 1xPBS, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.
More Info
-
Introduction
CB1 cannabinoid receptor-interacting protein 1 (CNRIP1) is a 164 amino acid protein and G-protein coupled receptor which is a member of the CNRIP family. The CNRIP1 interacts with the C-terminal tail of cannabinoid receptor 1. CNRIP1 is expressed in the brain tissue and, at low levels, in the testis. CNRIP1 is involved in appetite, synaptic plasticity, neuroprotection and analgesia.
-
Synonyms
Thymosin beta-4, T beta 4, Fx , TB4X, PTMB4, TMSB4.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Thymosin B4 Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thymosin B4 Human 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 Thymosin B4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
SDKPDMAEIE KFDKSKLKKT ETQEKNPLPS KETIEQEKQA GES
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.
- View Data Sheet
Name :
SPA-CysDescription:
Staphylococcal Protein-A Cys Recombinant
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
Product # :
PRO-1922Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
SPA-Cys Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain with a Cys on C-terminus. SPA-Cys is comprised of 5 IgG-binding domains E-D-A-B-C aligned in series containing 297 amino acids and having a molecular mass of 33.5kDa containing little or no carbohydrate. Cell wall binding region, cell membrane binding region and albumin binding region were removed to ensure the highest specific IgG binding.
Source
Escherichia Coli.
Formulation
SPA protein was lyophilized with no additives.
Purity
Greater than 98.0% as determined by: (a) Analysis by HPLC.(b) Analysis by SDS-PAGE.
More Info
-
Introduction
Protein A is a cell wall component produced by several strains of Staphylococcus aureus. The recombinant Protein A is genetically engineered protein and holds 5 IgG-binding regions of protein A. Recombinant Protein A functions basically the same as native Protein A and is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein A binds to human IgG1, IgG2 and IgG4, mouse IgG2a, IgG2b and IgG3 and rat IgG2c. Protein A also binds to total IgG from rabbit, pig, dog, cat, and guinea pig.
-
Synonyms
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized SPA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SPA 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 SPA in sterile 18MΩ-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
NAAQHDEAQQ NAFYQVLNMP NLNADQRNGF IQSLKDDPSQ SANVLGEAQK LNDSQAPKAD AQQNNFNKDQ QSAFYEILNM PNLNEAQRNG FIQSLKDDPS QSTNVLGEAK KLNESQAPKA DNNFNKEQQN AFYEILNMPN LNEEQRNGFI QSLKDDPSQS ANLLSEAKKL NESQAPKADN KFNKEQQNAF YEILHLPNLN EEQRNGFIQS LKDDPSQSAN LLAEAKKLND AQAPKADNKF NKEQQNAFYE ILHLPNLTEE QRNGFIQSLK DDPSVSKEIL AEAKKLNDAQ APKEEDC
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.
- View Data Sheet
Name :
Avidin RecombinantDescription:
Avidin Recombinant
Avidin, AVD, AVID.
Product # :
PRO-2597Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- purity
- biological activity
- More Info
Description
Recombinant Avidin produced in Plants is a polypeptide chain having a molecular mass of 66kDa and 16kda per subunit. The Recombinant Avidin is purified by affinity chromatographic techniques.
Source
Corn (Zea Mays).
Purity
Greater than 90% as visualized by SDS-PAGE.
Biological Activity
13.5 units/mg protein, 1 unit binds 1µg biotin.
More Info
-
Introduction
Avidin is a tetrameric protein of 4 identical subunits (homotetramer) which can bind to biotin with a high degree of affinity and specificity. The estimated molecular weight of Avidin in its tetrameric form is between 66-69 kDa. Avidin is produced in the oviducts of birds, reptiles and amphibians and is subsequently deposited in the whites of their eggs. In the chicken egg white, avidin makes up roughly 0.05% of total protein (approximately 1.8 mg per egg). 10% of Avidin’s molecular weight is ascribed to carbohydrate content which is composed of 4-5 mannose and 3 N-acetylglucosamine residues. Avidin has at least three distinctive oligosaccharide structural type which are similar in structure and composition. The dissociation constant (KD) of avidin is approximately 10-15M, making it one of the strongest known non-covalent bonds.
-
Synonyms
Avidin, AVD, AVID.
-
Physical Appearance
Sterile Filtered white lyophilized powder.
-
Stability
Lyophilized Recombinant Avidin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Recombinant Avidin 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 Recombinant Avidin in sterile 18MΩ-cm H2O not less than 100µg/ml or more than 10mg/ml 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.
- View Data Sheet
Name :
IgA Sec antibodyDescription:
IgA Secretory Component, Mouse Anti-Human
Product # :
ANT-174Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- formulation
- More Info
Formulation
1mg/ml in PBS (after reconstitution).
More Info
-
Solubility
Reconstitute with H20 to get a 1 mg/ml concentration. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
-
Immunogen
Purified hIgA.
-
Ig Subclass
Mouse IgG1.
-
Clone
NYRhIgA.
-
Note
This antibody will react against all human IgA subtypes.
-
Titer
By direct ELISA, 1:20,000 dilution will yield >1.0 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
-
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
-
Type
Mouse Anti Human Monoclonal.
-
Storage Procedures
In lyophilized form, for long periods, store at 4°C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.
-
Purification Method
Ion exchange column.
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.
- View Data Sheet
Name :
GlucagonDescription:
Glucagon Human
GLP1, GLP2, GRPP.
Product # :
HOR-286Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- formulation
- purity
- More Info
Description
Glucagon Human Synthetic is a single, non-glycosylated, polypeptide chain containing 29 amino acids and having a molecular mass of 3483 Dalton and the molecular formula is: C153H225N43O49S.The Glucagon is purified by proprietary chromatographic techniques.
Formulation
Glucagon peptide was formulated with no additives.
Purity
Greater than 96.0% as determined by RP-HPLC.
More Info
-
Introduction
Glucagon is an important hormone involved in carbohydrate metabolism. The hormone is synthesized and secreted from alpha cells (?-cells) of the islets of Langerhans, which are located in the endocrine portion of the pancreas. Glucagon is released when the glucose level in the blood is low (hypoglycemia), causing the liver to convert stored glycogen into glucose and release it into the bloodstream. The action of glucagon is thus opposite to that of insulin, which instructs the body's cells to take in glucose from the blood in times of satiation.
Glucagon is beneficial for the culture of some cell types. It has been used in some biochemical regulation studies of glycogenolysis in hepatocytes. It has been also been found to induce DNA replication in primary cultures of adult rat hepatocytes when used in combinations with EGF and Insulin. Glucagon increases the blood glucose concentration by promoting rapid breakdown of liver glycogen, and also acts to relax smooth muscle such as the gastrointestinal tract. -
Synonyms
GLP1, GLP2, GRPP.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Glucagon although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Glucagon 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 Glucagon in a sterile 1% HCl solution at a concentration of 0.1-1 mg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
His-Ser-Gln-Gly-Thr-Phe-Thr-Ser-Asp-Tyr-Ser-Lys-Tyr-Leu-Asp-Ser-Arg-Arg-Ala-Gln-Asp-Phe-Val-Gln-Trp-Leu-Met-Asn-Thr-OH.
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.
- View Data Sheet
Name :
S100A14 HumanDescription:
S100 Calcium Binding Protein A14 Human Recombinant
Protein S100-A14, S100 calcium-binding protein A14, S114, S100A14, S100A15, BCMP84.
Product # :
PRO-154Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
S100A14 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 124 amino acids (1-104 a.a.) and having a molecular mass of 13.8kDa. The S100A14 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The S100A14 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 2mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
S100A14 belongs to a subfamily of proteins related by EF-hand Ca2+ binding protein superfamily. The extracellular functions of the S100 family include the ability to boost neurite outgrowth, involvement in inflammation, and motility of tumor cells. S100A14 contains 2 EF-hand Ca2+-binding domains, a myristoylation motif, a glycosylation site, and a number of potential protein kinase phosphorylation sites. S100A14 is expressed at high levels in the colon and at moderate levels in the thymus, kidney, liver, small intestine, and lung.
-
Synonyms
Protein S100-A14, S100 calcium-binding protein A14, S114, S100A14, S100A15, BCMP84.
-
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 MGQCRSANAE DAQEFSDVER AIETLIKNFH QYSVEGGKET LTPSELRDLV TQQLPHLMPS NCGLEEKIAN LGSCNDSKLE FRSFWELIGE AAKSVKLERP VRGH.
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.
- View Data Sheet
Name :
DIRAS1 HumanDescription:
DIRAS family, GTP-binding RAS-like 1 Human Recombinant
GTP-binding protein Di-Ras1, Distinct subgroup of the Ras family member 1, Ras-related inhibitor of cell growth, Rig, Small GTP-binding tumor suppressor 1, DIRAS1, GBTS1, Di-Ras1, FLJ42681.
Product # :
PRO-256Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
DIRAS1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 215 amino acids (1-195a.a.) and having a molecular mass of 24.1 kDa. DIRAS1 protein is fused to a 20 amino acid His tag at N-terminus and is purified by standard chromatography.
Source
Escherichia Coli.
Formulation
DIRAS1 Human solution (1mg/ml) containing 20mM Tris-HCl buffer(pH 8.0) containing 20% glycerol, 1mM DTT, 0.1M NaCl and 1mM EDTA.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
DIRAS1 is a member of a distinct branch of the functionally diverse Ras superfamily of monomeric GTPases. DIRAS1 demonstrates low GTPase activity and exists mainly in the GTP-bound form. Ras proteins operate as binary molecular switches that control intracellular signaling networks. Ras-regulated signal pathways regulate such processes as actin cytoskeletal integrity, proliferation, differentiation, cell adhesion, apoptosis, and cell migration. Ras and ras-related proteins are frequently deregulated in cancers, leading to increased invasion and metastasis, and decreased apoptosis.
-
Synonyms
GTP-binding protein Di-Ras1, Distinct subgroup of the Ras family member 1, Ras-related inhibitor of cell growth, Rig, Small GTP-binding tumor suppressor 1, DIRAS1, GBTS1, Di-Ras1, FLJ42681.
-
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 MPEQSNDYRV VVFGAGGVGK SSLVLRFVKG TFRDTYIPTI EDTYRQVISC DKSVCTLQIT DTTGSHQFPA MQRLSISKGH AFILVFSVTS KQSLEELGPI YKLIVQIKGS VEDIPVMLVG KCDETQREV DTREAQAVAQ EWKCAFMETS AKMNYNVKEL FQELLTLETR RNMSLNIDGK RSGKQKRTDR KGKC.
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.
- View Data Sheet
Name :
Cardiac Actin BovineDescription:
Cardiac Actin Bovine
Actin alpha cardiac muscle 1, Alpha-cardiac actin, ACTC1, ACTC.
Product # :
PRO-519Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Ultra pure Cardiac Actin having a Molecular mass of 43,000 dalton.
Source
Bovine Heart.
Formulation
The protein was lyophilized from a 1mg/ml solution containing 10mM Tris-acetate buffer pH 8.0, 0.2mM CaCl2, 0.2mM ATP, 1mM DTT and 0.5% SDS.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
Alpha-cardiac actin belongs to the actin family which is comprised of three main groups of actin isoforms, alpha, beta, and gamma. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. Defects in the cardiac actin have been associated with idiopathic dilated cardiomyopathy (IDC) and familial hypertrophic cardiomyopathy (FHC).
-
Synonyms
Actin alpha cardiac muscle 1, Alpha-cardiac actin, ACTC1, ACTC.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Cardiac-Actin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Cardiac Actin 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 Cardiac Actin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Applications
Protein standard in 1D and 2D SDS gelelectrophoresis
Immunoassays
Immunization.
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.
- View Data Sheet
Name :
KEL MouseDescription:
Kell Metallo-Endopeptidase Mouse Recombinant
kell blood group antigen, kell blood group glycoprotein, Kell blood group, Kell blood group glycoprotein homolog, KEL, Kell, CD238 antigen, CD238, ECE3, Kell blood group-metalloendopeptidase, Kell blood group-metalloendopeptidase.
Product # :
ENZ-1158Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
KEL Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 674 amino acids (49-713 aa) and having a molecular mass of 76.3kDa.KEL is fused to a 9 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The KEL solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Kell blood group glycoprotein homolog or KEL, is an enzyme, part of the zinc endopeptidase of the neprilysin (NEP) group of proteins. KEL has a crucial part in the production of the potent bioactive ET-3, which also includes enzymes that are endothelin convertingenzymes (PEX, XCE, DINE &various NEP-like proteins). KEL uses a single disulfide bond to XK, a gated membranal transporter. The Kell antigen system that includes two proteins, is very crucial among blood group systems.
-
Synonyms
kell blood group antigen, kell blood group glycoprotein, Kell blood group, Kell blood group glycoprotein homolog, KEL, Kell, CD238 antigen, CD238, ECE3, Kell blood group-metalloendopeptidase, Kell blood group-metalloendopeptidase.
-
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
ADPIFRNCGP CPCETPVCME LLDHYLASGN RSVAPCTDFF SFACEKANGT SDSFQALTEE NKSRLWRLLE APGSWHLGSG EEKAFQFYNS CMDTDAIEAS GSGPLIQIIE ELGGWNITGN WTSLDFNQNL RLLMSQYGHF PFFRAYLRPH PAPPHTPIIQ IDQPEFDILL QQEQEQKVYA QILREYVTYL NRLGTLLGSN PQEAQQHASW SIVFTSRLFQ FLRPQQQQQA QDKLFHVVTI DELQEMAPAI DWLSCLQAIF TPMSLNSSQT LVVHDLDYLR NMSQLVEEGL LNHRESIQSY MILGLVDTLS PALDTKFQEA RRELIQELRK LKERPPLPAY PRWMKCVEQT GAFFEPTLAA LFVREAFGPS IQSAAMELFA EIKDAVIIRL KKLSWISEET QKEALNKLAQ LQVEMGAPKR AVKPDIATQE YNDIQLGPSF LQSFLSCVRS LRARNVQSFL QPFPYHRWQK SPWEVNAYYS ISDHMVVFPA GLLQPPFFHP GYPRAVNFGA AGSIMAHELL HIFYQLLLPG GCPACDTHVL QEALLCLERH YAAFPLPSIS SFNGSHTLLE NAADIGGVAI AFQAYSKRIV EHTGELTLPN LDLSPYQLFF RSYAQVMCRG LSSQDPQDPH SPPSLRVHGP LSNTPDFAKH FHCPRGTLLN PSARCKLWHH HHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CDH5 HumanDescription:
Cadherin 5 Human Recombinant
Cadherin 5, VE-Cadherin, Cadherin 5 Type 2 VE-Cadherin (Vascular Epithelium), CDH5, Cadherin 5 Type 2 (Vascular Endothelium), Vascular Endothelial Cadherin, 7B4 Antigen, Endothelial-Specific Cadherin, Cd144 Antigen, CD144 Antigen, Cadherin-5, CD144, 7B4.
Product # :
PRO-2384Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Cadherin 5 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 810 amino acids (29-599 a.a.) and having a molecular mass of 91.5kDa (Migrates at 70-100kDa on SDS-PAGE under reducing conditions). CDH5 is expressed with a 239 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
CDH5 solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) & 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Cadherin-5 (CDH5) belongs to the atypical/type 2 subgroup of Cadherin homophilic adhesion proteins. Cadherin-5 is a calcium-dependent cell-cell adhesion molecule, which is comprised of 5 extracellular cadherin repeats, a transmembrane region and a highly conserved cytoplasmic tail. Cadherin-5 protein plays a role in the formation, maturation and remodeling of the vascular wall. CDH5 is generally considered to be specific for vascular endothelia in which it is either the sole or the predominant cadherin, often co-existing with N-cadherin. Moreover, the CDH5 protein regulates or is regulated by VEGF R2, type 1 and type 2 TGF-beta receptors, and other endothelial junction proteins such as JAM-C, Claudin-5, and N-Cadherin. CDH5 also connects with alpha-catenin forming a link to the cytoskeleton. CDH5 functions jointly with KRIT1 to create and maintain correct endothelial cell polarity and vascular lumen. Furthermore, Cadherin-5 is essential for activation of PRKCZ and for the localization of phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction. The CDH5 gene is located in a gene cluster in a region on the long arm of chromosome 16 which is involved in loss of heterozygosity events in breast and prostate cancer.
-
Synonyms
Cadherin 5, VE-Cadherin, Cadherin 5 Type 2 VE-Cadherin (Vascular Epithelium), CDH5, Cadherin 5 Type 2 (Vascular Endothelium), Vascular Endothelial Cadherin, 7B4 Antigen, Endothelial-Specific Cadherin, Cd144 Antigen, CD144 Antigen, Cadherin-5, CD144, 7B4.
-
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
NPAQRDTHSL LPTHRRQKRD WIWNQMHIDE EKNTSLPHHV GKIKSSVSRK NAKYLLKGEY VGKVFRVDAE TGDVFAIERL DRENISEYHL TAVIVDKDTG ENLETPSSFT IKVHDVNDNW PVFTHRLFNA SVPESSAVGT SVISVTAVDA DDPTVGDHAS VMYQILKGKE YFAIDNSGRI ITITKSLDRE KQARYEIVVE ARDAQGLRGD SGTATVLVTL QDINDNFPFF TQTKYTFVVP EDTRVGTSVG SLFVEDPDEP QNRMTKYSIL RGDYQDAFTI ETNPAHNEGI IKPMKPLDYE YIQQYSFIVE ATDPTIDLRY MSPPAGNRAQ VIINITDVDE PPIFQQPFYH FQLKENQKKP LIGTVLAMDP DAARHSIGYS IRRTSDKGQF FRVTKKGDIY NEKELDREVY PWYNLTVEAK ELDSTGTPTG KESIVQVHIE VLDENDNAPE FAKPYQPKVC ENAVHGQLVL QISAIDKDIT PRNVKFKFIL NTENNFTLTD NHDNTANITV KYGQFDREHT KVHFLPVVIS DNGMPSRTGT STLTVAVCKC NEQGEFTFCE DMAAQVGVSI QLEPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGKHHHHHH.
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.
- View Data Sheet
Name :
LGALSL HumanDescription:
Lectin Galactoside-Binding-Like Human Recombinant
GRP, HSPC159, Galectin-related protein, Lectin galactoside-binding-like protein, LGALSL.
Product # :
PRO-1374Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
LGALSL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 195 amino acids (1-172a.a) and having a molecular mass of 21.4kDa. LGALSL is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
LGALSL protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
Galectins are a family of soluble b-galactoside-binding animal lectins that modulate cell-to-cell adhesion and cell-to-extracellular matrix interactions. Galectins also take part in tumor progression, pre-mRNA splicing and apoptosis. Galectin-related protein (LGALSL) is a 172 amino acid protein which holds one galectin domain. In spite of this, LGALSL does not appear to bind carbohydrates or lactose since the critical residues required for binding are not conserved.
-
Synonyms
GRP, HSPC159, Galectin-related protein, Lectin galactoside-binding-like protein, LGALSL.
-
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 MGSMAGSVAD SDAVVKLDDG HLNNSLSSPV QADVYFPRLI VPFCGHIKGG MRPGKKVLVM GIVDLNPESF AISLTCGDSE DPPADVAIEL KAVFTDRQLL RNSCISGERG EEQSAIPYFP FIPDQPFRVE ILCEHPRFRV FVDGHQLFDF YHRIQTLSAI DTIKINGDLQ ITKLG.
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.
- View Data Sheet
Name :
CGREF1 HumanDescription:
Cell Growth Regulator With EF-Hand Domain 1 Human Recombinant
Cell Growth Regulator With EF-Hand Domain 1, Cell Growth Regulatory Gene 11 Protein, Hydrophobestin, CGR11, Cell Growth Regulator With EF Hand Domain Protein 1, Cell Growth Regulator With EF Hand Domain 1, Cell growth regulator with EF hand domain protein 1.
Product # :
PRO-2154Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CGREF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 305 amino acids (20-301 a.a) and having a molecular mass of 32.3kDa. CGREF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CGREF1 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH7.4).
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
Cell Growth Regulator with EF-Hand Domain 1, also known as CGREF1 is a secreted calcium ion binding protein. CGREF1 includes two EF-hand domains & both EF-hands are essential for function. CGREF1 is most likely digested extracellularly by an unfamiliar serine protease generating extremely hydrophobic bioactive peptides. CGREF1 mediates cell-cell adhesion in a calcium-dependent manner. In addition, CGREF1 is capable to inhibit growth in more than a few cell lines.
-
Synonyms
Cell Growth Regulator With EF-Hand Domain 1, Cell Growth Regulatory Gene 11 Protein, Hydrophobestin, CGR11, Cell Growth Regulator With EF Hand Domain Protein 1, Cell Growth Regulator With EF Hand Domain 1, Cell growth regulator with EF hand domain protein 1.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSAPKDGVT RPDSEVQHQL LPNPFQPGQE QLGLLQSYLK GLGRTEVQLE HLSREQVLLY LFALHDYDQS GQLDGLELLS MLTAALAPGA ANSPTTNPVI LIVDKVLETQ DLNGDGLMTP AELINFPGVA LRHVEPGEPL APSPQEPQAV GRQSLLAKSP LRQETQEAPG PREEAKGQVE ARRESLDPVQ EPGGQAEADG DVPGPRGEAE GQAEAKGDAP GPRGEAGGQA EAEGDAPGPR GEAGGQAEAR ENGEEAKELP GETLESKNTQ NDFEVHIVQV ENDEI.
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.
- View Data Sheet
Name :
Haptoglobin (19-347) HumanDescription:
Haptoglobin (19-347 a.a) Human Recombinant
Haptoglobin, Zonulin, Haptoglobin alpha chain, Haptoglobin beta chain, Haptoglobin isoform 2 preproprotein, BP, HP2ALPHA2, HPA1S.
Product # :
PRO-1897Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Haptoglobin Human Recombinant produced in E. coli is a single polypeptide chain containing 352 amino acids (19-347) and having a molecular mass of 39.0 kDa. Haptoglobin is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Haptoglobin solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
-
Introduction
Haptoglogin participates in intestinal permeability, permitting intercellular tight junction disassembly, and controlling the equilibrium among tolerance and immunity to non-self antigens. Haptoglobin has antibacterial activity and takes part in modulating many aspects of the acute phase response. Haptoglobin is processed to yield both alpha and beta chains, which later unite as a tetramer to produce haptoglobin. Haptoglobin binds free hemoglobin (Hb) secreted from erythrocytes In blood plasma with high affinity and thus inhibits its oxidative activity. Further, the haptoglobin-hemoglobin complex is being removed by the reticuloendothelial system.
-
Synonyms
Haptoglobin, Zonulin, Haptoglobin alpha chain, Haptoglobin beta chain, Haptoglobin isoform 2 preproprotein, BP, HP2ALPHA2, HPA1S.
-
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 MGSVDSGNDV TDIADDGCPK PPEIAHGYVE HSVRYQCKNY YKLRTEGDGV YTLNNEKQWI NKAVGDKLPE CEAVCGKPKN PANPVQRILG GHLDAKGSFP WQAKMVSHHN LTTGATLINE QWLLTTAKNL FLNHSENATA KDIAPTLTLY VGKKQLVEIE KVVLHPNYSQ VDIGLIKLKQ KVSVNERVMP ICLPSKDYAE VGRVGYVSGW GRNANFKFTD HLKYVMLPVA DQDQCIRHYE GSTVPEKKTP KSPVGVQPIL NEHTFCAGMS KYQEDTCYGD AGSAFAVHDL EEDTWYATGI LSFDKSCAVA EYGVYVKVTS IQDWVQKTIA EN.
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.
- View Data Sheet
Name :
SAA1 HumanDescription:
Serum Amyloid A (APO-SAA1) Human Recombinant
Serum amyloid A protein, SAA, Amyloid protein A, Amyloid fibril protein AA, SAA1, SAA2, PIG4, TP53I4, MGC111216.
Product # :
CYT-787Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
SAA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 104 amino acids and having a molecular mass of 11.7kDa. The SAA1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SAA1 was lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris-HCl, pH 9.0 and 150mM NaCl.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity determined by a chemoattract bioassay using human monocytes is in a concentration range of 10-100 ng/ml.More Info
-
Introduction
SAA1 protein is an acute phase apolipoprotein reactant which is produced mostly by hepatocytes and under regulation of inflammatory cytokines. SAA1 (Serum amyloid A1) protein is produced mainly in the liver and circulates in low levels in the blood. The SAA1 seems to have a role in the immune system. SAA1 protein levels increase in the blood and other tissues under conditions of inflammation. SAA1 may facilitate the repair of injured tissues; it also acts as an antibacterial agent, and signals the migration of germ-fighting cells to sites of infection. SAA1 also functions as an apolipoprotein of the HDL complex.
Elevated levels of SAA1 ultimately affect secondary amyloidosis, extracellular amassing of amyloid fibrils, resulting from a circulating precursor, in a variety of tissues and organs. The most widespread type of amyloidosis appears secondary to chronic inflammatory disease, mainly rheumatoid arthritis. The SAA1 cleavage product a designated amyloid protein A is deposited systemically as amyloid in vital organs such as the liver, spleen, and kidneys in chronic inflammatory diseases patients. These deposits are extremely insoluble and resistant to proteolysis; they disrupt tissue structure and compromise performance. -
Synonyms
Serum amyloid A protein, SAA, Amyloid protein A, Amyloid fibril protein AA, SAA1, SAA2, PIG4, TP53I4, MGC111216.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized SAA1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SAA1 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 SAA1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
RSFFSFLGEA FDGARDMWRA YSDMREANYI GSDKYFHARG NYDAAKRGPG GVWAAEAISD ARENIQRFFG HGAEDSLADQ AANEWGRSGK DPNHFRPAGL PEKY.
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.
- View Data Sheet
Name :
OXLD1 HumanDescription:
Oxidoreductase-Like Domain Containing 1 Human Recombinant
C17orf90, Oxidoreductase-like domain-containing protein 1, OXLD1.
Product # :
PRO-2005Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
OXLD1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 125 amino acids (46-147a.a) and having a molecular mass of 13.4kDa. OXLD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
OXLD1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 50% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Oxidoreductase-Like Domain Containing 1, also known as OXLD1, is a Protein Coding gene which is associated with the lncRNA class. OXLD1 holds 1 Oxidoreductase-like domain.
-
Synonyms
C17orf90, Oxidoreductase-like domain-containing protein 1, OXLD1.
-
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 MGSPGAQAPD GRRKFGTDHV EVGSQAGADG TRPPKASLPP ELQPPTNCCM SGCPNCVWVE YADRLLQHFQ DGGERALAAL EEHVADENLK AFLRMEIRLH TRCGG.
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.
- View Data Sheet
Name :
GINS4 HumanDescription:
GINS Complex Subunit 4 Protein Human Recombinant
SLD5, GINS complex subunit 4, DNA replication complex GINS protein SLD5.
Product # :
PRO-1270Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
GINS4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 243 amino acids (1-223 a.a.) and having a molecular mass of 28.2kDa.GINS4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GINS4 protein solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl,20% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
GINS4, a member of the GINS4/SLD5 family, has a key part in the initiation of DNA replication, and progression of DNA replication forks. GINS4 is significant for GINS complex assembly. GINS complex connects favorably to singlestranded DNA. Recombinant human GINS4 protein, fused to His-tag at N-terminus was purified by using conventional chromatography techniques.
-
Synonyms
SLD5, GINS complex subunit 4, DNA replication complex GINS protein SLD5.
-
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 MTEEVDFLGQ DSDGGSEEVV LTPAELIERL EQAWMNEKFA PELLESKPEI VECVMEQLEH MEENLRRAKR EDLKVSIHQM EMERIRYVLS SYLRCRLMKI EKFFPHVLEK EKTRPEGEPS SLSPEELAFA REFMANTESY LKNVALKHMP PNLQKVDLFR AVPKPDLDSY VFLRVRERQE NILVEPDTDE QRDYVIDLEK GSQHLIRYKT IAPLVASGAV QLI
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.
- View Data Sheet
Name :
Epigen HumanDescription:
Epigen Human Recombinant
EPG, Epigen, PRO9904, ALGV3072, FLJ75542, EPGN, Epithelial mitogen.
Product # :
CYT-601Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Epigen Recombinant Human produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 72 amino acids and having a molecular mass of 7.9 kDa. Epigen is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
EPGN was lyophilized from 20mM PBS buffer pH-7.4 .
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells. The expected ED50 for this effect is less than 300 ng/ml, corresponding to a specific activity of > 3.3 ×103 IU/mg.
More Info
-
Introduction
EPGN is an EGF-related polypeptide growth factor that signals through the ErbB receptor-1. EPGN is produced in numerous tissues, including the testis, liver, heart and in certain tumor cells. EPGN is mitogenic for fibroblasts and epithelial cells. Human EPGN is originally synthesized as a glycosylated 14.7 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a mature soluble sequence.
-
Synonyms
EPG, Epigen, PRO9904, ALGV3072, FLJ75542, EPGN, Epithelial mitogen.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Epigen although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EPGN 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 Epigen in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
AVTVTPPITA QQADNIEGPI ALKFSHLCLE DHNSYCINGA CAFHHELEKA ICRCFTGYTG ERCEHLTLTS YA
-
Background
What is the molecular weight/Mw of EPIGEN Protein?
EPIGEN Protein has a total Mw of 7.9kDa.
What is the source or expression system of EPIGEN Protein?
Escherichia Coli.
What is the Purity of EPIGEN Protein?
EPIGEN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of EPIGEN Protein?
Determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells. The expected ED50 for this effect is less than 300 ng/ml, corresponding to a specific activity of > 3.3 ×103 IU/mg.
What is the amino acid sequence of EPIGEN Protein?
AVTVTPPITA QQADNIEGPI ALKFSHLCLE DHNSYCINGA CAFHHELEKA ICRCFTGYTG ERCEHLTLTS YA
What applications can EPIGEN Protein be used in?
EPIGEN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EPIGEN Protein?
The endotoxin level is minimal, EPIGEN 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.
- View Data Sheet
Name :
DKK3 Human, HEKDescription:
Dickkopf-Related Protein 3 Human Recombinant, HEK
Dickkopf 3 homolog (Xenopus laevis), dickkopf-related protein 3, regulated in glioma, RIG, RIG-like 7-1, RIG-like 5-6, Dkk-3, REIC.
Product # :
PRO-1638Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
DKK3 Human Recombinant is a single polypeptide chain containing 337 amino acids (22-350). DKK3 is fused to 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
DKK3 was lyophilized from a 0.2µM filtered solution of 20mM PB and 150mM NaCl, pH 7.2.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
Dickkopf-related protein 3 (DKK3) belongs to the DKK protein family including Dkk-1, 2, 3 and -4. DKK3 is a 350 amino acid secreted glycoprotein which is comprised of an N-terminal signal peptide and 2 conserved cysteine-rich domains that are separated by a 12 amino acid linker region. DKK3 is involved in embryonic development through its inhibition of the WNT signaling pathway. DKK3 gene expression is decreased in a variety of cancer cell lines and it may act as a tumor suppressor gene.
-
Synonyms
Dickkopf 3 homolog (Xenopus laevis), dickkopf-related protein 3, regulated in glioma, RIG, RIG-like 7-1, RIG-like 5-6, Dkk-3, REIC.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized DKK3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution DKK3 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 DKK3 in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
APAPTATSAPVKPGPALSYPQEEATLNEMFREVEELMEDTQHKLRSAVEEMEAEEAAA
KASSEVNLANLPPSYHNETNTDTKVGNNTIHVHREIHKITNNQTGQMVFSETVITSVG
DEEGRRSHECIIDEDCGPSMYCQFASFQYTCQPCRGQRMLCTRDSECCGDQLCVWGHC
TKMATRGSNGTICDNQRDCQPGLCCAFQRGLLFPVCTPLPVEGELCHDPASRLLDLIT
WELEPDGALDRCPCASGLLCQPHSHSLVYVCKPTFVGSRDQDGEILLPREVPDEYEVG
SFMEEVRQELEDLERSLTEEMALGEPAAAAAALLGGEEIVDHHHHHH.
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.