Search: 902 results found for "BID"

Description:

Brain-Derived Neurotrophic Factor Human Recombinant

Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

Product # :

CYT-207

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Activity

Description

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

Source

Escherichia Coli.

Formulation

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

Purity

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

Biological Activity

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

Activity

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Introduction
BDNF promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. BDNF is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the cns. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (ltp), long-term depression (ltd), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.
Synonyms
Brain-Derived Neurotrophic Factor, BDNF, MGC34632.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BDNF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized BDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.
Background
Final Thoughts
Although more research is needed on the safety and effectiveness of BDNF human recombinant, trials suggest that this laboratory-produced protein may be effective in managing and treating several neurological and psychiatric disorders. It's important for experts to stay up to date on the latest developments and research to learn more about potential risks and benefits.
What is the molecular weight/Mw of BDNF Protein?
BDNF Protein has a total Mw of 27kDa.

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

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

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

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

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

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

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

Description:

CDGSH Iron Sulfur Domain 1, Mouse Anti Human

CDGSH Iron Sulfur Domain 1, Chromosome 10 Open Reading Frame 70, CDGSH Iron Sulfur Domain-Containing Protein 1, Zinc Finger CDGSH-Type Domain 1, C10orf70, ZCD1, MitoNEET , MDS029.

Product # :

ANT-061

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Formulation

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

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Introduction
CISD1 protein holds a CDGSH iron-sulfur domain and is known to bind a redox-active [2Fe-2S] cluster. CISD1 is restricted to the outer membrane of mitochondria and takes part in oxidation regulation.
Synonyms
CDGSH Iron Sulfur Domain 1, Chromosome 10 Open Reading Frame 70, CDGSH Iron Sulfur Domain-Containing Protein 1, Zinc Finger CDGSH-Type Domain 1, C10orf70, ZCD1, MitoNEET , MDS029.
Physical Appearance
Sterile Filtered colorless solution.
Immunogen
Anti-human CISD1 mAb, clone PAT1A8A, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human CISD1 protein 32-108 amino acids purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and Kappa light chain.
Clone
PAT1A8A.
Applications
The antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.
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
CISD1 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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

Description:

Maltose Binding Protein E.coli Recombinant, His Tag

Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.

Product # :

PRO-2322

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Description

Recombinant E.Coli MBP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 410 amino acids (27-392 a.a) and having a molecular mass of 44.9kDa. MBP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MBP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Maltose Binding Protein is a member of the maltose/maltodextrin system of E.Coli, which is accountable for the uptake and efficient catabolism of maltodextrins. The maltose/maltodextrin is a complex regulatory and transport system involving many proteins and protein complexes.
MBP elevates the yield of its fusion partner in many cases and is often able to promote the solubility of polypeptides to which it is fused.
Synonyms
Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.
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 MGSMKIEEGK LVIWINGDKG YNGLAEVGKK FEKDTGIKVT VEHPDKLEEK FPQVAATGDG PDIIFWAHDR FGGYAQSGLL AEITPDKAFQ DKLYPFTWDA VRYNGKLIAY PIAVEALSLI YNKDLLPNPP KTWEEIPALD KELKAKGKSA LMFNLQEPYF TWPLIAADGG YAFKYENGKY DIKDVGVDNA GAKAGLTFLV DLIKNKHMNA DTDYSIAEAA FNKGETAMTI NGPWAWSNID TSKVNYGVTV LPTFKGQPSK PFVGVLSAGI NAASPNKELA KEFLENYLLT DEGLEAVNKD KPLGAVALKS YEEELAKDPR IAATMENAQK GEIMPNIPQM SAFWYAVRTA VINAASGRQT VDEALKDAQT NSSSNNNNNN NNNNLGIEGR.

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.

Description:

Hepatitis C Virus Core, Biotin Recombinant

Product # :

HCV-242

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Description

The E.coli derived recombinant Biotin Labeled protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119, having an MW of 22kDa. The protein is fused to a beta-galactosidase (114 kDa) at the N-terminus.

Formulation

20mM Tris-HCl pH 8 and 8M urea.

Purity

Protein is >95% pure as determined by SDS-PAGE.

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Introduction
HCV is a small 50nm, enveloped, single-stranded, positive sense RNAvirus in the family Flaviviridae.
HCV has a high rate of replication with approximately one trillion particles produced each day in an infected individual. Due to lack of proofreading by the HCV RNA polymerase, the HCV has an exceptionally high mutation rate, a factor that may help it elude the host's immune response. Hepatitis C virus is classified into six genotypes(1-6) with several subtypes within each genotype. The preponderance and distribution of HCV genotypes varies globally. Genotype is clinically important in determining potential response to interferon-based therapy and the required duration of such therapy. Genotypes 1 and 4 are less responsive to interferon-based treatment than are the other genotypes (2, 3, 5 and 6).
Stability
HCV Core although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Applications
Antigen in ELISA and Western blots, excellent antigen for detection of HCV with minimal specificity problems.
Specificity
Immunoreactive with sera of HCV-infected individuals.
Purification Method
HCV Core protein was purified by proprietary chromatographic technique.

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

Description:

Diazepam Binding Inhibitor Mouse Recombinant

Acyl-CoA-binding protein, ACBP, Diazepam-binding inhibitor, DBI, Endozepine, EP, Dbi.

Product # :

PRO-2527

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Description

DBI Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 110 amino acids (1-87 a.a) and having a molecular mass of 12.4kDa. DBI is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

DBI protein solution (1mg/ml) contains Phosphate buffer saline (pH7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
DBI, also known as Acyl-CoA-binding protein isoform 2, is a diazepam binding inhibitor, which is regulated by hormones. DBI participates in lipid metabolism and in the displacement of beta-carbolines & benzodiazepines, which modulate signal transduction at type A gamma-aminobutyric acid receptors located in brain synapses. Moreover, during adipocyte differentiation the expression of DBI is significantly induced. DBI preforms as an acyl-CoA pool former and regulates LCFA (long-chain fatty acids) metabolism in peripheral tissues.
Synonyms
Acyl-CoA-binding protein, ACBP, Diazepam-binding inhibitor, DBI, Endozepine, EP, Dbi.
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 MGSMSQAEFD KAAEEVKRLK TQPTDEEMLF IYSHFKQATV GDVNTDRPGL LDLKGKAKWD SWNKLKGTSK ESAMKTYVEK VDELKKKYGI

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Description:

MHC CLASS II, (I-E) Mouse Antibody, Biotin

Product # :

ANT-298

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Formulation

1mg/ml in PBS (after reconstitution).

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Introduction
HC Class II is consists of 2 membrane spanning proteins. Each of these proteins is roughly 30 kDa, and has of two Globular domains, Alpha-1, Alpha-2, Beta-1 and Beta-2. The two regions farthest away from the membrane are alpha-1 and beta-1. The two proteins link without Covalent Bonds. The MHC Class II protein mainly presents peptides, which have been digested from external sources. MHC Class II is normally only expressed by Antigen Presenting Cells (APC) which digest foreign protein. Within the RER the alpha and beta proteins of the molecule, associate with each other, while a third protein called the "invariant chain," is necessary for stabilizing the complex, without it, they will not associate. The MHC-invariant complex is then passed from the RER, into and out of, the Golgi body. It fuses with an Endocytic compartment, where an external protein has been sampled and degraded.
Solubility
Reconstitute with of H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
Purified mouse LN B cells (C3H anti-C57Bl6).
Ig Subclass
Mouse IgG2a.
Clone
NYRmI-E.
Applications
Cytotoxic and staining antibody. For staining, use 10ml/1,000,000 cells. Titer for cytotoxicity should be determined by the investigator.
Specificity
Recognizes most MHC I-E class II haplotypes Reacts with H-2k, H-2d, H-2p and H-2r.
Available Conjugates
This antibody is also available as unconjugated antibody and conjugated to FITC.
Type
Mouse Antibody Monoclonal.
Storage Procedures
Lyophilized: store at 4°C. 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.

Description:

SARS MERS Spike Receptor Binding Domain Recombinant, Active

Middle East respiratory syndrome coronavirus, Human betacoronavirus 2c EMC/2012, MERS-CoV, MERS, MERSCoV RBD, MERS RBD, receptor binding domain, RBD, Spike RBD protein, Spike glycoprotein, S glycoprotein, E2, Peplomer protein

Product # :

SARS-060

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Description

SARS MERS RBD Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 258 amino acids (358-606 aa) and having a molecular mass of 28.2kDa. SARS MERS RBD is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The SARS MERS RBD solution (0.5mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured by its binding ability in a functional ELISA with Human DPPIV/CD26 (CAT# enz-1187).

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Synonyms
Middle East respiratory syndrome coronavirus, Human betacoronavirus 2c EMC/2012, MERS-CoV, MERS, MERSCoV RBD, MERS RBD, receptor binding domain, RBD, Spike RBD protein, Spike glycoprotein, S glycoprotein, E2, Peplomer protein
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
ADPSGVYSVS SFEAKPSGSV VEQAEGVECD FSPLLSGTPP QVYNFKRLVF TNCNYNLTKL LSLFSVNDFT CSQISPAAIA SNCYSSLILD YFSYPLSMKS DLSVSSAGPI SQFNYKQSFS NPTCLILATV PHNLTTITKP LKYSYINKCS RLLSDDRTEV PQLVNANQYS PCVSIVPSTV WEDGDYYRKQ LSPLEGGGWL VASGSTVAMT EQLQMGFGIT VQYGTDTNSV CPKLEFANDT KIASQLGNCV EYHHHHHH.
Background
The severe acute respiratory syndrome coronavirus (SARS-CoV) and Middle East respiratory syndrome coronavirus (MERS-CoV) have posed significant global health threats in recent years. Central to their pathogenesis is the interaction between the viral spike proteins and host cell receptors. This research aims to investigate the receptor binding domain (RBD) of SARS and MERS spike proteins and its implications for viral entry and the development of therapeutic interventions. Understanding the molecular mechanisms underlying viral-host interactions can pave the way for targeted therapeutic strategies against these deadly coronaviruses.
Structure and Function of SARS and MERS Spike RBD:
The spike proteins of SARS-CoV and MERS-CoV are critical for viral entry into host cells. These proteins consist of two subunits: S1, responsible for receptor binding, and S2, involved in membrane fusion. The receptor binding domain (RBD) within the S1 subunit specifically interacts with host cell receptors, enabling viral attachment and entry. The RBDs of SARS and MERS spike proteins exhibit unique structural features and binding affinities for their respective receptors.
Interaction with ACE2 and DPP4 Receptors:
The SARS-CoV spike protein RBD interacts with the angiotensin-converting enzyme 2 (ACE2) receptor, which is abundantly expressed in the respiratory tract. The binding of SARS-CoV RBD to ACE2 facilitates viral entry into host cells. On the other hand, the MERS-CoV spike protein RBD interacts with the dipeptidyl peptidase 4 (DPP4) receptor, predominantly expressed in the lungs and other tissues. The ACE2 and DPP4 receptors play crucial roles in determining the host range and tissue tropism of SARS and MERS coronaviruses.
Implications for Viral Pathogenesis:
The binding of SARS and MERS spike RBDs to their respective receptors triggers conformational changes in the spike protein, leading to membrane fusion and subsequent viral entry. This process is crucial for viral replication and the spread of infection within the host. The specificity and affinity of the RBD-receptor interaction influence viral tropism, tissue damage, and disease severity. Understanding the determinants of RBD-receptor binding can provide insights into viral pathogenesis and potential therapeutic targets.
Development of Therapeutic Interventions:
The RBD of SARS and MERS spike proteins represents a promising target for the development of antiviral therapeutics. Several strategies have been explored, including monoclonal antibodies and small molecule inhibitors, to disrupt the RBD-receptor interaction and inhibit viral entry. These approaches aim to block the binding interface between the spike RBD and the host receptor, thereby preventing viral attachment and entry. Additionally, vaccine development efforts have focused on generating neutralizing antibodies against the RBD to elicit protective immune responses.
Conclusion:
The investigation of the receptor binding domain (RBD) of SARS and MERS spike proteins sheds light on the molecular mechanisms underlying viral entry and pathogenesis. The specific interactions between the spike RBD and host cell receptors play a crucial role in determining viral tropism and tissue damage. Targeting the RBD-receptor interaction holds promise for the development of effective therapeutics against SARS-CoV, MERS-CoV, and potentially other related coronaviruses. Further research and development efforts are needed to exploit the potential of the spike RBD as a therapeutic target and to combat future coronavirus outbreaks.

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Description:

Tick-Borne Encephalitis Virus gE Middle Recombinant

Product # :

TBE-283

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Description

The E.coli derived recombinant protein contains the Tick-borne Encephalitis Virus glycoprotein E middle regions, 50-250 amino acids.

Source

Escherichia Coli.

Formulation

20mM MES pH 6.5, 8M urea, 200mM NaCl and 0.05% Tween-20.

Purity

Encephalitis protein is >95% pure as determined by 10% PAGE (coomassie staining).

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Introduction
TBE is caused by tick-borne encephalitis virus (TBEV), a member of the family Flaviviridae.
A closely related virus in Far Eastern Eurasia, Russian spring-summer encephalitis virus (RSSEV).
The family Flaviviridae includes other tick-borne viruses are closely related to TBEV and RSSEV, such as Omsk hemorrhagic fever virus & Kyasanur Forest virus.
Louping ill virus is also a member of this family.
Physical Appearance
Sterile Filtered clear solution.
Stability
Encephalitis protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Applications
Encephalitis antigen is suitable for ELISA and Western blots, excellent antigen for detection of Tick-borne encephalitis virus with minimal specificity problems.
Specificity
Immunoreactive with sera of encephalitis virus infected individuals.
Purification Method
Encephalitis protein was purified by proprietary chromatographic technique.

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

Description:

Dysbindin (Dystrobrevin Binding Protein 1) Domain Containing 2 Human Recombinant

Dysbindin domain-containing protein 2, Casein kinase-1 binding protein, CK1BP, HSMNP1, DBNDD2, C20orf35.

Product # :

PRO-1167

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Description

DBNDD2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 185 amino acids (1-161 a.a) and having a molecular mass of 20.1kDa (Molecular weight on SDS-PAGE will appear higher).DBNDD2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

DBNDD2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Dysbindin domain-containing protein 2 (DBNDD2) is a member of the dysbindin family. DBNDD2 regulates the activity of casein kinase-1 and inhibits CSNK1D autophosphorylation (in vitro). DBNDD2 also interacts with CSNK1D and CSNK1E. DBNDD2 is detected in brain.
Synonyms
Dysbindin domain-containing protein 2, Casein kinase-1 binding protein, CK1BP, HSMNP1, DBNDD2, C20orf35.
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 MGSHMDPNPR AALERQQLRL RERQKFFEDI LQPETEFVFP LSHLHLESQR PPIGSISSME VNVDTLEQVE LIDLGDPDAA DVFLPCEDPP PTPQSSGMDN HLEELSLPVP TSDRTTSRTS SSSSSDSSTN LHSPNPSDDG ADTPLAQSDE EEERGDGGAE PGACS.

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Description:

Bone Morphogenetic protein Receptor-1A Human Recombinant, IgG-His

BMPR1A, 10q23del, ACVRLK3, ALK3, CD292, SKR5, Bone Morphogenetic Protein Receptor Type 1A, Bone Morphogenetic Protein Receptor, Type IA, Serine/Threonine-Protein Kinase Receptor R5, Activin Receptor-Like Kinase 3, BMP Type-1A Receptor, EC 2.7.11.30, ALK-3, Bone Morphogenetic Protein Receptor Type-1A, Activin A Receptor, Type II-Like Kinase 3, CD292 Antigen, EC 2.7.1.

Product # :

CYT-1005

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Description

BMPR1A Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 371 amino acids (24-152a.a.) and having a molecular mass of 41.4kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).BMPR1A is fused with a 242 amino acids hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

BMPR1A protein solution (1mg/ml) contains Phosphate Buffered Saline (pH7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
The bone morphogenetic protein (BMP) receptors are a family of transmembrane serine/threonine kinases that include the type I receptors BMPR1A and BMPR1B and the type II receptor BMPR2. These receptors are also closely related to the activin receptors, ACVR1 and ACVR2. The ligands of these receptors are members of the TGF-beta superfamily. TGF-betas and activins transduce their signals through the formation of heteromeric complexes with 2 different types of serine (threonine) kinase receptors: type I receptors of about 50-55 kD and type II receptors of about 70-80 kD. Type II receptors bind ligands in the absence of type I receptors, but they require their respective type I receptors for signaling, whereas type I receptors require their respective type II receptors for ligand binding.
Synonyms
BMPR1A, 10q23del, ACVRLK3, ALK3, CD292, SKR5, Bone Morphogenetic Protein Receptor Type 1A, Bone Morphogenetic Protein Receptor, Type IA, Serine/Threonine-Protein Kinase Receptor R5, Activin Receptor-Like Kinase 3, BMP Type-1A Receptor, EC 2.7.11.30, ALK-3, Bone Morphogenetic Protein Receptor Type-1A, Activin A Receptor, Type II-Like Kinase 3, CD292 Antigen, EC 2.7.1.
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
ADPQNLDSML HGTGMKSDSD QKKSENGVTL APEDTLPFLK CYCSGHCPDD AINNTCITNG HCFAIIEEDD QGETTLASGC MKYEGSDFQC KDSPKAQLRR TIECCRTNLC NQYLQPTLPP VVIGPFFDGS IRLEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH H.
Background
Research Paper on Bone Morphogenetic Protein Receptor-1A Human Recombinant, IgG-His, Monomer, HEK
Abstract:
Welcome to the fascinating world of Bone Morphogenetic Protein Receptor-1A Human Recombinant, IgG-His, Monomer (BMPR-1A HR) in Human Embryonic Kidney Cells (HEK). This paper explores the vital role of BMPR-1A HR in cellular responses. As a critical receptor in the transforming growth factor-beta (TGF-β) superfamily, BMPR-1A HR guides cellular differentiation and tissue development. Join us as we uncover the molecular mechanisms behind BMPR-1A HR signaling in HEK cells and explore its synonyms, along with its interactions with key cytokines, including Tumor Necrosis Factor-alpha (TNF-α) and Tumor Necrosis Factor-alpha Superfamily Member 2 (TNFα SF2 or TNFSF2).
Introduction:
Step into the captivating realm of BMPR-1A HR! This paper introduces the remarkable BMPR-1A HR and its crucial role in shaping cellular responses. As researchers, we are driven by curiosity to understand how BMPR-1A HR influences cellular behavior and contributes to tissue growth.
BMPR-1A HR Signaling in HEK Cells:
Unravel the intricate dance of BMPR-1A HR signaling within HEK cells! We explore the complex process of ligand-receptor binding, which initiates both the canonical SMAD-dependent and non-canonical SMAD-independent pathways, regulating gene transcription, cell proliferation, and differentiation.
Extensive Description of BMPR-1A HR:
As researchers, we provide a comprehensive overview of BMPR-1A HR's structural characteristics and unique attributes. With its Monomeric nature and the IgG-His tag, crucial for detection and purification, we delve into the intricacies of BMPR-1A HR.
Influential Role in Cellular Responses:
Marvel at BMPR-1A HR's influential role as a critical mediator of cellular responses within HEK cells! Witness how it skillfully modulates cellular differentiation, driving the expression of key differentiation markers like DIF, impacting diverse cellular pathways.
Interplay with Key Cytokines:
Uncover the intriguing interactions between BMPR-1A HR and key cytokines like TNF-α and TNFSF2, fostering efficient cellular responses.
Therapeutic Implications and Tissue Development:
Explore the potential therapeutic implications of BMPR-1A HR in tissue development. We envision exciting possibilities of utilizing BMPR-1A HR in regenerative medicine, offering hope for enhanced tissue development and repair.
Conclusion:
As we conclude our exploration of BMPR-1A HR in HEK cells, we anticipate a promising future where BMPR-1A HR with an IgG-His tag becomes an invaluable tool in biomedical research, promoting human well-being.
What is the molecular weight/Mw of BMPR1A Protein?
BMPR1A Protein has a total Mw of 41.4kDa.

What is the source or expression system of BMPR1A Protein?
Sf9, Baculovirus cells.

What is the Purity of BMPR1A Protein?
BMPR1A Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of BMPR1A Protein?
The biological functionality of BMPR1A Protein will be determined in the future.

What is the amino acid sequence of BMPR1A Protein?
ADPQNLDSML HGTGMKSDSD QKKSENGVTL APEDTLPFLK CYCSGHCPDD AINNTCITNG HCFAIIEEDD QGETTLASGC MKYEGSDFQC KDSPKAQLRR TIECCRTNLC NQYLQPTLPP VVIGPFFDGS IRLEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH H.

What applications can BMPR1A Protein be used in?
BMPR1A Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BMPR1A Protein?
The endotoxin level is minimal, BMPR1A 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.

Description:

Maltose Binding Protein E.coli Recombinant

Product # :

PRO-616

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Description

Maltose Binding Protein E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 387 amino acids (27-392) with additional 20aa linker and having a molecular mass of 42kDa.

Source

Escherichia Coli.

Formulation

The Maltose Binding Protein solution (1 mg/ml) contains 20mM Tris-HCl pH-8.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Maltose Binding Protein is a member of the maltose/maltodextrin system of E.Coli, which is accountable for the uptake and efficient catabolism of maltodextrins. The maltose/maltodextrin is a complex regulatory and transport system involving many proteins and protein complexes.
MBP elevates the yield of its fusion partner in many cases and is often able to promote the solubility of polypeptides to which it is fused.
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
MKIEEGKLVI WINGDKGYNG LAEVGKKFEK DTGIKVTVEH PDKLEEKFPQ VAATGDGPDI IFWAHDRFGG YAQSGLLAEI TPDKAFQDKL YPFTWDAVRY NGKLIAYPIAVEALSLIYNK DLLPNPPKTW EEIPALDKEL KAKGKSALMF NLQEPYFTWP LIAADGGYAF KYENGKYDIK DVGVDNAGAK AGLTFLVDLI KNKHMNADTD YSIAEAAFNK GETAMTINGP WAWSNIDTSK VNYGVTVLPT FKGQPSKPFV GVLSAGINAA SPNKELAKEF LENYLLTDEG LEAVNKDKPL GAVALKSYEE ELAKDPRIAA TMENAQKGEI MPNIPQMSAF WYAVRTAVIN AASGRQTVDE ALKDAQTNSS SNNNNNNNNN NLGIEGR.

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.

Description:

B cell Activating Factor Human Recombinant, His Tag

BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.

Product # :

CYT-545

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sds-page

Description

BLyS Human Recombinant fused to His tag at N-terminus produced in E.Coli is a single, non-glycosylated polypeptide chain containing 190 amino acids (134-285 a.a.) and having a molecular mass of 21 kDa. BAFF is fused to a 38 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Recombinant His Tag BAFF contains PBS pH-7.4 and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

sds-page

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Introduction
Binds to tnfrsf13b/taci and tnfrsf17/bcma. tnfsf13/april binds to the same 2 receptors, together, they form a 2 ligands -2 receptors pathway involved in the stimulation of b- and t-cell function and the regulation of humoral immunity. a third b-cell specific baff-receptor (baffr/br3) promotes the survival of mature b-cells and the b-cell response.
B Lymphocyte Stimulator functions as a potent B-cell growth factor in costimulation assays.
Administration of BAFF Human recombinant to mice disrupts splenic B-cell and T-cell zones and results in elevated levels of serum immunoglobulin.
Synonyms
BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.
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 KDRWGSHMAV QGPEETVTQD CLQLIADSET PTIQKGSYTF VPWLLSFKRG SALEEKENKI LVKETGYFFI YGQVLYTDKT YAMGHLIQRK KVHVFGDELS LVTLFRCIQN MPETLPNNSC YSAGIAKLEE GDELQLAIPR ENAQISLDGD VTFFGALKLL
Background
What is the molecular weight/Mw of BLYS Protein?
BLYS Protein has a total Mw of 21kDa.

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

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

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

What is the amino acid sequence of BLYS Protein?
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMAV QGPEETVTQD CLQLIADSET PTIQKGSYTF VPWLLSFKRG SALEEKENKI LVKETGYFFI YGQVLYTDKT YAMGHLIQRK KVHVFGDELS LVTLFRCIQN MPETLPNNSC YSAGIAKLEE GDELQLAIPR ENAQISLDGD VTFFGALKLL

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

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

Description:

BCL2/Adenovirus E1B 19kDa Interacting Protein 1 Human Recombinant

BCL2/Adenovirus E1B 19kDa Interacting Protein 1, NIP1, BCL2/Adenovirus E1B 19 KDa Protein-Interacting Protein 1, Transformation-Related Gene 8 Protein, TRG-8, BCL2/Adenovirus E1B 19kD-Interacting Protein 1, Vesicle Transport Protein SEC20, SEC20L, SEC20, Vesicle transport protein SEC20.

Product # :

PRO-2150

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Description

BNIP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids (1-199 a.a) and having a molecular mass of 25.2kDa. BNIP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BNIP1 protein solution (1.0 mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
BNIP1 belongs to the of the BCL2/adenovirus E1B 19 kd-interacting protein (BNIP) family. BNIP1 interacts with the E1B 19 kDa protein, which defends cells from virally-induced cell death. In addition, BNIP1 interacts with E1B 19 kDa-like sequences of BCL2 which is an additional apoptotic protector. Adding up, BNIP1 is implicated in vesicle transport into the endoplasmic reticulum. Alternative splicing results of BNIP1 in four protein products with identical N- and C-termini have been found.
Synonyms
BCL2/Adenovirus E1B 19kDa Interacting Protein 1, NIP1, BCL2/Adenovirus E1B 19 KDa Protein-Interacting Protein 1, Transformation-Related Gene 8 Protein, TRG-8, BCL2/Adenovirus E1B 19kD-Interacting Protein 1, Vesicle Transport Protein SEC20, SEC20L, SEC20, Vesicle transport protein SEC20.
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 MGSMAAPQDV HVRICNQEIV KFDLEVKALI QDIRDCSGPL SALTELNTKV KEKFQQLRHR IQDLEQLAKE QDKESEKQLL LQEVENHKKQ MLSNQASWRK ANLTCKIAID NLEKAELLQG GDLLRQRKTT KESLAQTSST ITESLMGISR MMAQQVQQSE EAMQSLVTSS RTILDANEEF KSMSGTIQLG RKLITKYNRR EL.

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.

Description:

Complement Component 4 Binding Protein, Beta Human Recombinant

C4b-binding protein beta chain, C4BPB, C4BP.

Product # :

PRO-1174

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Description

C4BPB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 260 amino acids (18-252 a.a) and having a molecular mass of 29kDa.C4BPB is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

C4BPB protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol and 0.15M NaCl.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Complement Component 4 Binding Protein, Beta (C4BPB) belongs to a superfamily of proteins composed primarily of tandemly arrayed short consensus repeats of approximately 60 amino acids. C4BPB has a regulatory role in the coagulation system also, mediated via the beta-chain binding of protein S, a vitamin K-dependent protein which functions as a cofactor of activated protein C. A single, unique beta-chain of the C4BPB assembles with 7 identical alpha-chains into the principal isoform of C4BPB, which is a multimeric protein that controls activation of the complement cascade via the classical pathway. C4BPB binds as a cofactor to C3b/C4b inactivator (C3bINA), which subsequently hydrolyzes the complement fragment C4b. In addition, C4BPB accelerates the degradation of the C4bC2a complex (C3 convertase) by detaching the complement fragment C2a. Furthermore, C4BPB interacts with anticoagulant protein S and with serum amyloid P component.
Synonyms
C4b-binding protein beta chain, C4BPB, C4BP.
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 MGSHMSDAEH CPELPPVDNS IFVAKEVEGQ ILGTYVCIKG YHLVGKKTLF CNASKEWDNT TTECRLGHCP DPVLVNGEFS SSGPVNVSDK ITFMCNDHYI LKGSNRSQCL EDHTWAPPFP ICKSRDCDPP GNPVHGYFEG NNFTLGSTIS YYCEDRYYLV GVQEQQCVDG EWSSALPVCK LIQEAPKPEC EKALLAFQES KNLCEAMENF MQQLKESGMT MEELKYSLEL KKAELKAKLL.

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.

Description:

Sonic HedgeHog Human Recombinant

SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.

Product # :

CYT-676

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Description

Sonic HedgeHog Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids and having a molecular mass of 20.2kDa. The Cys at position 2 has been substituted with 2 Ile’s.

Source

Escherichia Coli.

Formulation

SHH is lyophilized from 10mM Na3PO4, pH 7.5.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED50 is measured by the dose-dependent induction of alkaline phosphatase production by CCL-226 fibroblasts and is 1.47μg/ml corresponding to a specific activity of 680U/mg.

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Introduction
Recombinant Human Sonic Hedgehog is part of a small group of secreted proteins that are vital for development in both vertebrates and invertebrates. 3 mammalian hedgehog genes (sonic, desert, Indian) share about 60% homology. The Human Sonic Hedgehog is 99% homologous to the mouse gene. Sonic HedgeHog is a protein that is vital in guding the early embryo. It has been associated as the major inductive signal in patterning of the ventral neural tube, the anterior-posterior limb axis, and the ventral somites. Sonic HedgeHog binds to the patched receptor, which functions in association with smoothened, to activate the transcription of target genes. In the absence of sonic HedgeHog, patched receptor represses the constitutive signaling activity of smoothened. Sonic HedgeHog also regulates another factor, the gli oncogene. Sonic HedgeHog intercellular signal is essential for a various patterning events during development: signal produced by the notochord that induces ventral cell fate in the neural tube and somites, and the polarizing signal for patterning of the anterior-posterior axis of the developing limb bud. Sonic HedgeHog exhibits both floor plate- and motor neuron-inducing activity. Mutations in a long-range Sonic HedgeHog enhancer located in an intron of the limb region 1 gene result in preaxial polydactyly.
Synonyms
SHH, HHG-1, HHG1, Sonic hedgehog protein, TPT, HLP3, HPE3, SMMCI, TPTPS, MCOPCB5.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Human Sonic HedgeHog although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Sonic HedgeHog 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 SHH in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MIIGPGRGFG KRRHPKKLTP LAYKQFIPNV AEKTLGASGR YEGKISRNSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDKLNALAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRALDITTS DRDRSKYGML ARLAVEAGFD WVYYESKAHI HCSVKAENSV AAKSGGCFP

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.

Description:

Activin-A Rat Recombinant

Inhba, Inhibin beta A, FSH releasing protein.

Product # :

CYT-147

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Description

Active form Activin-A Rat Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.

Source

E.Coli.

Formulation

Rat Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.02% TFA.

Purity

Greater than 95% as obsereved by SDS-PAGE.

Biological Activity

Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml

More Info

Introduction
Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
Physical Appearance
Lyophilized freeze dried powder.
Stability
Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-A 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
Rat INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
Background
What is the molecular weight / Mw of Activin A Protein?
Activin A Protein has a total Mw of 26.2 kDa.

What is the source or expression system of Activin A Protein?
Ecoli

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

What is the Biological Activity of Activin A Protein?
Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml corresponding to a specific activity of 110,000units/mg.

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

What is the amino acid sequence of ACTIVIN A Protein?
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.

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

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.

Description:

Sorbitol Dehydrogenase Human Recombinant

EC 1.1.1.14, SORD1, SORD, L-iditol 2-dehydrogenase, DHSO, Sorbitol Dehydrogenase,SDH, (R,R)-butanediol dehydrogenase, L-iditol 2-dehydrogenase, Polyol dehydrogenase, Ribitol dehydrogenase, RDH, Xylitol dehydrogenase, XDH

Product # :

ENZ-1151

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Description

SORD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 357 amino acids (1-357a.a.) and having a molecular mass of 38.3kDa.SORD is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The SORD solution (0.5mg/ml) contains 10% glycerol, 20mM Tris-HCl buffer (pH 8.5) and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Specific activity > 15unit/mg. Defined by the amount of enzyme that catalyze the reduction 1.0 umole of D-fructose to D-sorbitol per minute at pH 7.5 at 37˚C.

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Introduction
SORD, also referred to as sorbitol dehydrogenase, belongs to the zinc-containing alcohol dehydrogenase family. It is widely produced. The lens of the eyeand the kidney are the protein highest production areas. Zinc-dependent interconversion of polyols, like sorbitol and xylitol, are enzymatically catalysed to their respective ketoses by SORD.
Synonyms
EC 1.1.1.14, SORD1, SORD, L-iditol 2-dehydrogenase, DHSO, Sorbitol Dehydrogenase,
SDH, (R,R)-butanediol dehydrogenase, L-iditol 2-dehydrogenase, Polyol dehydrogenase, Ribitol dehydrogenase, RDH, Xylitol dehydrogenase, XDH
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
MAAAAKPNNL SLVVHGPGDL RLENYPIPEP GPNEVLLRMH SVGICGSDVH YWEYGRIGNF IVKKPMVLGH EASGTVEKVG SSVKHLKPGD RVAIEPGAPR ENDEFCKMGR YNLSPSIFFC ATPPDDGNLC RFYKHNAAFC YKLPDNVTFE EGALIEPLSV GIHACRRGGV TLGHKVLVCG AGPIGMVTLL VAKAMGAAQV VVTDLSATRL SKAKEIGADL VLQISKESPQ EIARKVEGQL GCKPEVTIEC TGAEASIQAG IYATRSGGTL VLVGLGSEMT TVPLLHAAIR EVDIKGVFRY CNTWPVAISM LASKSVNVKP LVTHRFPLEK ALEAFETFKK GLGLKIMLKC DPSDQNP

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.

Description:

Inhibitor of DNA Binding 1 Human Recombinant

bHLHb24, ID, DNA-binding protein inhibitor ID-1, Class B basic helix-loop-helix protein 24, Inhibitor of DNA binding 1, ID1.

Product # :

PRO-1426

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Description

ID1 Human Recombinant produced in E. coli is a single polypeptide chain containing 178 amino acids (1-155) and having a molecular mass of 18.5kDa. ID1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The ID1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Inhibitor of DNA Binding 1 (ID1) is a helix-loop-helix protein which can form heterodimers with members of the basic HLH family of transcription factors. ID1 is lacking DNA binding activity and thus can inhibit the DNA binding and transcriptional activation ability of basic HLH proteins with which it interacts. ID1 participates in cell growth, senescence, and differentiation.
Synonyms
bHLHb24, ID, DNA-binding protein inhibitor ID-1, Class B basic helix-loop-helix protein 24, Inhibitor of DNA binding 1, ID1.
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 MGSMKVASGS TATAAAGPSC ALKAGKTASG AGEVVRCLSE QSVAISRCAG GAGARLPALL DEQQVNVLLY DMNGCYSRLK ELVPTLPQNR KVSKVEILQH VIDYIRDLQL ELNSESEVGT PGGRGLPVRA PLSTLNGEIS ALTAEAACVP ADDRILCR.

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.

Description:

Activin-A Human Recombinant, Active

Inhba, Inhibin beta A, FSH releasing protein.

Product # :

CYT-145

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Description

Active form Activin-A Human Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.

Source

E.Coli.

Formulation

Human Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.1% TFA.

Purity

Greater than 95% as obsereved by SDS-PAGE.

Biological Activity

Biological activity is assessed by the ability to induce cytotoxicity of MPC-11 cells and was found to be 8.95ng/ml corresponding to a specific activity of 1.1 x 10⁵ units/mg.

More Info

Introduction
Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
Physical Appearance
Lyophilized freeze dried powder.
Stability
Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-A 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
Human INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
Background
Title: Research on Activin A Human Recombinant: Molecular Characteristics, Signaling Pathways, Physiological Functions, and Therapeutic Potential
Introduction:
Activin A, a member of the transforming growth factor-beta (TGF-β) superfamily, is a multifunctional cytokine that plays a significant role in various biological processes in the human body. Its involvement in diverse physiological and pathological functions has garnered considerable attention in scientific research. This paper aims to provide an overview of Activin A, encompassing its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential.
Activin A is encoded by the INHBA gene and is produced as a precursor protein that undergoes post-translational modifications to generate the mature form. The mature Activin A protein consists of two β-subunits held together by disulfide bonds. These structural features contribute to its functional properties and interactions with specific receptors.
Upon binding to its cell surface receptors, Activin A triggers intracellular signaling cascades, leading to various cellular responses. Canonical SMAD-dependent pathway as well as non-SMAD pathways, such as MAPK/ERK, PI3K/Akt, and JNK signaling, are activated by Activin A. The intricate network of signaling pathways enables Activin A to regulate diverse biological processes, including cell proliferation, differentiation, apoptosis, and tissue homeostasis.
Activin A exerts its physiological functions in a tissue-specific manner. It plays a critical role in embryonic development, particularly in organogenesis and patterning. Additionally, Activin A is involved in reproductive biology, where it participates in folliculogenesis, spermatogenesis, and hormonal regulation. It also contributes to neural development, immune system modulation, and skeletal homeostasis.
The multifunctional properties of Activin A have positioned it as a potential therapeutic target for various diseases. Its involvement in cancer, neurodegenerative disorders, fibrosis, and reproductive disorders has prompted extensive research to explore its therapeutic potential. Understanding the molecular mechanisms underlying Activin A's actions provides valuable insights for developing innovative therapeutic strategies.
In conclusion, Activin A is a versatile cytokine with diverse roles in human biology. This research aims to deepen our understanding of its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential. By elucidating the complexities of Activin A, we strive to pave the way for novel therapeutic interventions in various human diseases.

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Description:

Dysbindin (Dystrobrevin Binding Protein 1) Domain Containing 1 Human Recombinant

Dysbindin domain-containing protein 1, DBNDD1.

Product # :

PRO-1162

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Description

DBNDD1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 182 amino acids (1-158 a.a) and having a molecular mass of 19.6kDa (Molecular weight on SDS-PAGE will appear higher).DBNDD1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

DBNDD1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.1M NaCl and 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Dysbindin domain-containing protein 1 (DBNDD1) is a member of the dysbindin family.
Synonyms
Dysbindin domain-containing protein 1, DBNDD1.
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 MGSHMEPPEG AGTGEIVKEA EVPQAALGVP AQGTGDNGHT PVEEEVGGIP VPAPGLLQVT ERRQPLSSVS SLEVHFDLLD LTELTDMSDQ ELAEVFADSD DENLNTESPA GLHPLPRAGY LRSPSWTRTR AEQSHEKQPL GDPERQATVL DTFLTVERPQ ED.

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.

Description:

Interleukin-18 Binding Protein Human Recombinant

Interleukin 18 Binding Protein, MC51L-53L-54L Homolog Gene Product, Tadekinig-Alfa, IL-18BP, IL18BPa, Interleukin-18-binding protein, Tadekinig-alfa.

Product # :

CYT-728

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Description

IL18BP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 187 amino acids (31-194 a.a) and having a molecular mass of 20kDa. IL18BP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

IL18BP protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Interleukin-18 Binding Protein (IL18BP) serves as an inhibitor of the proinflammatory cytokine, IL18. IL18BP binds IL18, inhibits the binding of IL18 to its receptor, and consequently inhibits IL18-induced IFN-gamma production, resulting in reduced T-helper type 1 immune responses. The IL18BP protein is constitutively expressed and secreted in mononuclear cells. Elevated levels of IL18BP protein are detected in the intestinal tissues of patients with Crohn's disease.
Synonyms
Interleukin 18 Binding Protein, MC51L-53L-54L Homolog Gene Product, Tadekinig-Alfa, IL-18BP, IL18BPa, Interleukin-18-binding protein, Tadekinig-alfa.
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 MGSTPVSQTT TAATASVRST KDPCPSQPPV FPAAKQCPAL EVTWPEVEVP LNGTLSLSCV ACSRFPNFSI LYWLGNGSFI EHLPGRLWEG STSRERGSTG TQLCKALVLE QLTPALHSTN FSCVLVDPEQ VVQRHVVLAQ LWAGLRATLP PTQEALPSSH SSPQQQG.

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Description:

Activin-A Mouse Recombinant

Inhba, Inhibin beta A, FSH releasing protein.

Product # :

CYT-146

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Description

Active form Activin-A Murine Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.

Source

E.Coli.

Formulation

Mouse Activin-A lyophilized from a concentrated 1mg/ml protein solution containing 0.1% TFA.

Purity

Greater than 95% as obsereved by SDS-PAGE.

Biological Activity

Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml corresponding to a specific activity of 1.1 x 10⁵ units/mg.

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Introduction
Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
Physical Appearance
Lyophilized freeze dried powder.
Stability
Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-A 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
Murine INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
Background
What is the molecular weight / Mw of Activin A Protein?
Activin A Protein has a total Mw of 26.2 kDa.
What is the source or expression system of Activin A Protein?
Ecoli

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

What is the Biological Activity of Activin A Protein?
Biological activity is assessed by the ability to induce cytoxicity of MPC-11 cells and was found to be 8.8ng/ml corresponding to a specific activity of 110,000 units/mg.

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

What is the amino acid sequence of ACTIVIN A Protein?
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.

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

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Description:

Phenazine Biosynthesis-Like Protein Domain Containing Human Recombinant

Phenazine biosynthesis-like domain-containing protein, MAWD-binding protein, Unknown protein 32 from 2D-page of liver tissue, PBLD, MAWBP, MAWDBP, FLJ14767, FLJ35507.

Product # :

PRO-010

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Description

PBLD 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 308 amino acids (1-288 a.a.) and having a molecular mass of 33.9kDa. The PBLD is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PBLD solution (1 mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
PBLD is member of the phenazine biosynthesis-like protein (PhzF) family. PBLD which is expressed in most tissues is the only representative of the PhzF family in the human genome. PBLD participates in the MAPK signaling pathway. PBLD is involved in multiple basic cellular functions, its expression is elevated in several disease processes, including folate deficiency and hypotension.
Synonyms
Phenazine biosynthesis-like domain-containing protein, MAWD-binding protein, Unknown protein 32 from 2D-page of liver tissue, PBLD, MAWBP, MAWDBP, FLJ14767, FLJ35507.
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 MKLPIFIADA FTARAFRGNP AAVCLLENEL DEDMHQKIAR EMNLSETAFI RKLHPTDNFA QSSCFGLRWF TPASEVPLCG HATLASAAVL FHKIKNMNST LTFVTLSGEL RARRAEDGIV LDLPLYPAHP QDFHEVEDLI KTAIGNTLVQ DICYSPDTQK LLVRLSDVYN RSFLENLKVN TENLLQVENT GKVKGLILTL KGEPGGQTQA FDFYSRYFAP WVGVAEDPVT GSAHAVLSSY WSQHLGKKEM HAFQCSHRGG ELGISLRPDG RVDIRGGAAV VLEGTLTA.

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.

Description:

Rat Anti-Mouse CD44, Biotinylated

MDU2, MDU3, MIC4, CDW44, CSPG8, HCELL, HUTCH-I, Phagocytic glycoprotein I, PGP-1, Extracellular matrix receptor-III, ECMR-III, Hermes antigen, Hyaluronate receptor, Heparan sulfate proteoglycan, Epican) CDw44.

Product # :

ANT-294

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Shipped at Room temp

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Formulation

1mg/ml in PBS (after reconstitution).

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Introduction
CD44 is a cell-surface glycoprotein that plays a role in cell-cell interactions, cell adhesion and migration. CD44 is a receptor for hyaluronic acid and also interacts with other ligands, such as osteopontin, collagens, and matrix metalloproteinases. CD44 participates in a wide variety of cellular functions such as lymphocyte activation, recirculation and homing, hematopoiesis, and tumor metastasis.
CD44 and CD49d are putative activity markers and CD44 a potential novel therapeutic target in multiple sclerosis. Increased CD44 antigen is associated with relapses in non-small cell lung cancers.
Synonyms
MDU2, MDU3, MIC4, CDW44, CSPG8, HCELL, HUTCH-I, Phagocytic glycoprotein I, PGP-1, Extracellular matrix receptor-III, ECMR-III, Hermes antigen, Hyaluronate receptor, Heparan sulfate proteoglycan, Epican) CDw44.
Solubility
Reconstitute with of H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
CD44 enriched mouse LN T cells.
Ig Subclass
Rat IgG.
Clone
mCD44.
Applications
Staining, immunohistochemistry. For staining, use 10µl/1,000,000 cells. Titer for IH should be determined by the investigator.
Available Conjugates
This antibody is also available unconjugated and conjugated to FITC.
Type
Rat Anti Mouse Monoclonal.
Storage Procedures
Lyophilized: store at 4°C. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.
Purification Method
Protein A.

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.

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