Search: 1000 results found for "Autophagy Related"

Description:

Aspartic Peptidase, Retroviral-Like 1 Human Recombinant

Retroviral-like aspartic protease 1, Skin-specific retroviral-like aspartic protease, SASPase, Skin aspartic protease, TPA-inducible aspartic proteinase-like protein, TAPS, ASPRV1, SASP, MUNO.

Product # :

ENZ-659

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Description

ASPRV1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 159 amino acids (191-326) and having a molecular mass of 17.2kDa.ASPRV1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The ASPRV1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Aspartic Peptidase, Retroviral-Like 1 (ASPRV1) is a protein which contains one peptidase A2 domain. ASPRV1 undergoes autocleavage which is essential for activation of the protein. ASPRV1 is expressed mostly in the granular layer of the epidermis and inner root sheath of hair follicles and localized to membrane region. In the psoriatic skin, ASPRV1 is expressed throughout the stratum corneum. In the ulcerated skin, ASPRV1 is expressed in the stratum granulosum of intact epidermis; however it is virtually nonexistent from ulcerated regions. In addition, ASPRV1 is expressed in differentiated areas of squamous cell carcinomas but not in the undifferentiated tumors.
Synonyms
Retroviral-like aspartic protease 1, Skin-specific retroviral-like aspartic protease, SASPase, Skin aspartic protease, TPA-inducible aspartic proteinase-like protein, TAPS, ASPRV1, SASP, MUNO.
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 MGSSMGKGYY LKGKIGKVPV RFLVDSGAQV SVVHPNLWEE VTDGDLDTLQ PFENVVKVAN GAEMKILGVW DTAVSLGKLK LKAQFLVANA SAEEAIIGTD VLQDHNAILD FEHRTCTLKG KKFRLLPVGG SLEDEFDLE.

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:

Non-Metastatic Cells 4 Human Recombinant

Non-metastatic cells 4, nm23-H4, NM23H4, Nucleoside diphosphate kinase D, NDK, NDPKD, NDP kinase mitochondrial, EC 2.7.4.6, NDPK-D.

Product # :

PRO-219

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Description

NME4 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 176 amino acids (33-187a.a.) and having a molecular mass of 19.6kDa. The NME4 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The NME4 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 40% glycerol and 0.2M NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
NME4 is a member of the NDK family. NME4 are ubiquitous enzymes which catalyze transfer of gamma-phosphates, using a phosphohistidine intermediate, between nucleoside and dioxynucleoside tri- and diphosphates. The enzymes are products of the nm23 gene family that include NME4. NME4 has a key part in the synthesis of nucleoside triphosphates other than ATP.
Synonyms
Non-metastatic cells 4, nm23-H4, NM23H4, Nucleoside diphosphate kinase D, NDK, NDPKD, NDP kinase mitochondrial, EC 2.7.4.6, NDPK-D.
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 MPSWTRERTL VAVKPDGVQR RLVGDVIQRF ERRGFTLVGM KMLQAPESVL AEHYQDLRRK PFYPALIRYM SSGPVVAMVW EGYNVVRASR AMIGHTDSAE AAPGTIRGDF SVHISRNVIH ASDSVEGAQR EIQLWFQSSE LVSWADGGQH SSIHPA.

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:

SH3 And Cysteine Rich Domain Human Recombinant

SH3 and cysteine rich domain, STAC, STAC1, SH3 and cysteine-rich domain-containing protein, Src homology 3 and cysteine-rich domain-containing protein.

Product # :

PRO-2010

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Description

STAC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 425 amino acids (1-402 a.a.) and having a molecular mass of 46.9kDa.STAC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
SH3 and Cysteine Rich Domain, which is also known as STAC, holds one phorbol-ester/DAG-type zinc finger and one SH3 domain. STAC takes part in a neuron-specific signal transduction.
Synonyms
SH3 and cysteine rich domain, STAC, STAC1, SH3 and cysteine-rich domain-containing protein, Src homology 3 and cysteine-rich domain-containing 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
MGSSHHHHHH SSGLVPRGSH MGSMIPPSSP REDGVDGLPK EAVGAEQPPS PASTSSQESK LQKLKRSLSF KTKSLRSKSA DNFFQRTNSE DMKLQAHMVA EISPSSSPLP APGSLTSTPA RAGLHPGGKA HAFQEYIFKK PTFCDVCNHM IVGTNAKHGL RCKACKMSIH HKCTDGLAPQ RCMGKLPKGF RRYYSSPLLI HEQFGCIKEV MPIACGNKVD PVYETLRFGT SLAQRTKKGS SGSGSDSPHR TSTSDLVEVP EEANGPGGGY DLRKRSNSVF TYPENGTDDF RDPAKNINHQ GSLSKDPLQM NTYVALYKFV PQENEDLEMR PGDIITLLED SNEDWWKGKI QDRIGFFPAN FVQRLQQNEK IFRCVRTFIG CKEQGQITLK ENQICVSSEE EQDGFIRVLS GKKKGLIPLD VLENI.

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:

Bone Morphogenetic Protein-7 Human Recombinant, His Tag

Osteogenic Protein 1, OP-1, BMP-7, Bone morphogenetic protein 7, BMP7, OP1.

Product # :

CYT-629

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Description

BMP7 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 148 amino acids (293-431) and having a molecular mass of 16.8 kDa. The BMP-7 is fused to 8 amino acid His Tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BMP-7 protein (0.5mg/ml) solution contains 10mM sodium citrate pH3.5 and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
The bone morphogenetic proteins (BMPs) are a family of secreted signaling molecules that can induce ectopic bone growth. Many BMPs are part of the transforming growth factor-beta (TGFB) superfamily. BMPs were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. Based on its expression early in embryogenesis, the BMP encoded by this gene has a proposed role in early development. In addition, the fact that this BMP is closely related to BMP5 and BMP7 has lead to speculation of possible bone inductive activity.
Synonyms
Osteogenic Protein 1, OP-1, BMP-7, Bone morphogenetic protein 7, BMP7, OP1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
Amino Acid Sequence
MSTGSKQRSQ NRSKTPKNQE ALRMANVAEN SSSDQRQACK KHELYVSFRD LGWQDWIIAP EGYAAYYCEG ECAFPLNSYM NATNHAIVQTLVHFINPETV PKPCCAPTQL NAISVLYFDD SSNVILKKYR NMVVRACGCH LEHHHHHH.
Background
Research Paper on Bone Morphogenetic Protein-7 Human Recombinant, His Tag, Monomer, HEK
Abstract:
Step into the fascinating world of Bone Morphogenetic Protein-7 Human Recombinant, His Tag, Monomer (BMP-7 HR) in Human Embryonic Kidney Cells (HEK). In this research paper, we embark on an exciting journey to uncover the wonders of BMP-7 HR and its significance in cellular differentiation. As a pivotal member of the transforming growth factor-beta (TGF-β) superfamily, BMP-7 HR holds immense potential in tissue regeneration and development. Join us as we delve into the intricate molecular mechanisms of BMP-7 HR signaling in HEK cells while also exploring its friendly interactions with key cytokines, including Tumor Necrosis Factor-alpha (TNF-α) and Tumor Necrosis Factor-alpha Superfamily Member 2 (TNFα SF2 or TNFSF2).
Introduction:
Welcome to the world of BMP-7 HR! In this section, we introduce the remarkable BMP-7 HR and its essential role in guiding cellular differentiation. Let's get to know our loyal companion, Human Embryonic Kidney Cells (HEK), as they help us unveil the secrets of BMP-7 HR signaling.
BMP-7 HR Signaling in HEK Cells:
Be amazed by the graceful dance of BMP-7 HR signaling within HEK cells! Uncover the captivating process of ligands binding to specific receptors, setting the stage for both the canonical SMAD-dependent and non-canonical SMAD-independent pathways. This harmonious interplay orchestrates various cellular processes, including gene transcription, cell proliferation, and differentiation.
Influential Role in Cellular Differentiation:
Watch in awe as BMP-7 HR takes center stage as a master conductor of cellular differentiation within HEK cells. Marvel at its ability to promote osteogenic differentiation, leading to the expression of vital osteogenic markers like RUNX2 and Osteocalcin. But that's not all! Join us in exploring BMP-7 HR's versatile nature, influencing other forms of differentiation, such as chondrogenic and adipogenic pathways.
Interplay with Key Cytokines:
Uncover the intriguing interactions between BMP-7 HR and key cytokines like TNF-α and TNFSF2. Witness how BMP-7 HR modulates the expression and activity of these cytokines, hinting at potential cross-talk between BMP-7 HR and inflammatory pathways, fostering a harmonious cellular environment.
Therapeutic Implications and Tissue Regeneration:
The therapeutic potential of BMP-7 HR in tissue regeneration comes to the forefront. Together, we explore the exciting possibilities of utilizing BMP-7 HR in regenerative medicine, offering hope for healing and tissue repair. As we navigate this path, we also address challenges, such as optimal dosage, innovative delivery methods, and safety considerations, ensuring the best outcomes.
Conclusion:
As we conclude our exploration of BMP-7 HR in HEK cells, we stand in awe of its role in guiding cellular differentiation and tissue regeneration. Equipped with this knowledge, we look forward to a future where BMP-7 HR opens doors to innovative applications in regenerative medicine, making a positive impact on human health and well-being.
What is the molecular weight/Mw of BMP7 Protein?
BMP7 Protein has a total Mw of 16.8kDa.

What is the source or expression system of BMP7 Protein?
Escherichia Coli.

What is the Purity of BMP7 Protein?
BMP7 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of BMP7 Protein?
The biological functionality of BMP7 Protein will be determined in the future.

What is the amino acid sequence of BMP7 Protein?
MSTGSKQRSQ NRSKTPKNQE ALRMANVAEN SSSDQRQACK KHELYVSFRD LGWQDWIIAP EGYAAYYCEG ECAFPLNSYM NATNHAIVQTLVHFINPETV PKPCCAPTQL NAISVLYFDD SSNVILKKYR NMVVRACGCH LEHHHHHH.

What applications can BMP7 Protein be used in?
BMP7 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BMP7 Protein?
The endotoxin level is minimal, BMP7 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:

Translational Activator of Mitochondrially Encoded Cytochrome C Oxidase Human Recombinant

Translational Activator Of Mitochondrially Encoded Cytochrome C Oxidase, CCDC44, Coiled-Coil Domain-Containing Protein 44, Coiled-Coil Domain Containing 44, Clone HQ0477 PRO0477p, Translational Activator Of Cytochrome C Oxidase 1, Translational Activator Of Mitochondrially-Encoded Cytochrome C Oxidase I.

Product # :

PRO-1746

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Description

TACO1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 260 amino acids (61-297 a.a) and having a molecular mass of 28.8kDa.TACO1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TACO1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Translational activator of mitochondrially encoded cytochrome c oxidase I (TACO1) belongs to the TACO1 family. TACO1 is a mitochondrial protein which functions as a translational activator of mitochondrially-encoded cytochrome c oxidase 1. Mutations in this gene are associated with Leigh syndrome.
Synonyms
Translational Activator Of Mitochondrially Encoded Cytochrome C Oxidase, CCDC44, Coiled-Coil Domain-Containing Protein 44, Coiled-Coil Domain Containing 44, Clone HQ0477 PRO0477p, Translational Activator Of Cytochrome C Oxidase 1, Translational Activator Of Mitochondrially-Encoded Cytochrome C Oxidase I.
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).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSNKWSKVR HIKGPKDVER SRIFSKLCLN IRLAVKEGGP NPEHNSNLAN ILEVCRSKHM PKSTIETALK MEKSKDTYLL YEGRGPGGSS LLIEALSNSS HKCQADIRHI LNKNGGVMAV GARHSFDKKG VIVVEVEDRE KKAVNLERAL EMAIEAGAEDVKETEDEEER NVFKFICDAS SLHQVRKKLD SLGLCSVSCA LEFIPNSKVQ LAEPDLEQAA HLIQALSNHE DVIHVYDNIE

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:

Family with Sequence Similarity 49, Member B Human Recombinant

BM-009, L1, Protein FAM49B, FAM49B.

Product # :

PRO-1411

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Description

FAM49B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 347amino acids (1-324 a.a) and having a molecular mass of 39.1kDa. FAM49B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

FAM49B protein solution (1mg/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
Family with Sequence Similarity 49, Member B (FAM49B) is a member of the FAM49 family. In the latest genome-wide transcriptional analysis, a gene signature was identified for multiple sclerosis (MS), which reverted back to normal during pregnancy. The reversion was mostly evident for seven genes: SOCS2, TNFAIP3, NR4A2, CXCR4, POLR2J, FAM49B, and STAG3L1, most of which are negative regulators of inflammation.
Synonyms
BM-009, L1, Protein FAM49B, FAM49B.
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 MGSMGNLLKV LTCTDLEQGP NFFLDFENAQ PTESEKEIYN QVNVVLKDAE GILEDLQSYR GAGHEIREAI QHPADEKLQE KAWGAVVPLV GKLKKFYEFS QRLEAALRGL LGALTSTPYS PTQHLEREQA LAKQFAEILH FTLRFDELKM TNPAIQNDFS YYRRTLSRMR INNVPAEGEN EVNNELANRM SLFYAEATPM LKTLSDATTK FVSENKNLPI ENTTDCLSTM ASVCRVMLET PEYRSRFTNE ETVSFCLRVM VGVIILYDHV HPVGAFAKTS KIDMKGCIKV LKDQPPNSVE GLLNALRYTT KHLNDETTSK QIKSMLQ.

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:

Chromobox Homolog 5 Human Recombinant

Chromobox homolog 5 (HP1 alpha homolog, Drosophila), Heterochromatin protein 1 homolog alpha, HP1Hs alpha, HP1 alpha homolog.

Product # :

PRO-1062

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Description

CBX5 Human Recombinant produced in E. coli is a single polypeptide chain containing 215 amino acids (1-191) and having a molecular mass of 24.8kDa.CBX5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The CBX5 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, 1mM DTT and 30% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
CBX5 belongs to the heterochromatin protein family. CBX5 is enriched in the heterochromatin and linked with centromeres. CBX5 takes part in the creation of functional kinetochore by interaction with important kinetochore proteins. CBX5 has a pseudogene situated on chromosome 3. Additionaly, The CBX5 proteins reconnect with chromatin at the end of mitosis, as Histone H3 is dephosphorylated.
Synonyms
Chromobox homolog 5 (HP1 alpha homolog, Drosophila), Heterochromatin protein 1 homolog alpha, HP1Hs alpha, HP1 alpha homolog.
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 MGSHMGKKTK RTADSSSSED EEEYVVEKVL DRRVVKGQVE YLLKWKGFSE EHNTWEPEKN LDCPELISEF MKKYKKMKEG ENNKPREKSE SNKRKSNFSN SADDIKSKKK REQSNDIARG FERGLEPEKI IGATDSCGDL MFLMKWKDTD EADLVLAKEA NVKCPQIVIA FYEERLTWHA YPEDAENKEK ETAKS.

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:

Killer Cell Lectin-Like Receptor Subfamily B, Member 1 Human Recombinant

Killer cell lectin-like receptor subfamily B member 1, Natural killer cell surface protein P1A, C-type lectin domain family 5 member B, CD161 antigen, HNKR-P1a, CLEC5B, NKR, NKR-P1.

Product # :

PRO-1189

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Description

KLRB1 Human Recombinant produced in E. coli is a single polypeptide chain containing 183 amino acids (67-225) and having a molecular mass of 21.0 kDa.KLRB1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The KLRB1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 4M urea and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
KLRB1 has an inhibitory role on natural killer (NK) cells cytotoxicity which are lymphocytes who facilitate cytotoxicity and secrete cytokines subsequent to immune stimulation. Some genes of the C-type lectin superfamily, like the rodent NKRP1 family of glycoproteins, are expressed by NK cells and take part in NK cell function regulation. KLRB1 holds an extracellular domain with a few characteristic motifs of C-type lectins, a transmembrane domain, and a cytoplasmic domain. Due to its external C terminus KLRB1 is considered to be a type II membrane protein.
Synonyms
Killer cell lectin-like receptor subfamily B member 1, Natural killer cell surface protein P1A, C-type lectin domain family 5 member B, CD161 antigen, HNKR-P1a, CLEC5B, NKR, NKR-P1.
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 MGSMQKSSIE KCSVDIQQSR NKTTERPGLL NCPIYWQQLR EKCLLFSHTV NPWNNSLADC STKESSLLLI RDKDELIHTQ NLIRDKAILF WIGLNFSLSE KNWKWINGSF LNSNDLEIRG DAKENSCISI SQTSVYSEYC STEIRWICQK ELTPVRNKVY PDS

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Description:

Guanine Nucleotide Binding Protein Alpha Z Polypeptide Human Recombinant

Guanine Nucleotide Binding Protein (G Protein) Alpha Z Polypeptide, G(X) Alpha Chain, Guanine Nucleotide-Binding Protein G(Z) Subunit Alpha, Gz-Alpha, Transducin Alpha.

Product # :

PRO-1225

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Description

GNAZ Human Recombinant produced in E. coli is a single polypeptide chain containing 375 amino acids (1-355) and having a molecular mass of 43.0 kDa.GNAZ is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The GNAZ solution (1mg/1ml) contains 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
Guanine nucleotide-binding protein G(z) subunit alpha (GNAZ) belongs to the G protein subfamily which mediates signal transduction in pertussis toxin-insensitive systems. GNAZ has a role in maintaining the ionic balance of perilymphatic and endolymphatic cochlear fluids. G proteins are involved as modulators or transducers in a variety of transmembrane signaling systems.
Synonyms
Guanine Nucleotide Binding Protein (G Protein) Alpha Z Polypeptide, G(X) Alpha Chain, Guanine Nucleotide-Binding Protein G(Z) Subunit Alpha, Gz-Alpha, Transducin Alpha.
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 MGCRQSSEEK EAARRSRRID RHLRSESQRQ RREIKLLLLG TSNSGKSTIV KQMKIIHSGG FNLEACKEYK PLIIYNAIDS LTRIIRALAA LRIDFHNPDR AYDAVQLFAL TGPAESKGEI TPELLGVMRR LWADPGAQAC FSRSSEYHLE DNAAYYLNDL ERIAAADYIP TVEDILRSRD MTTGIVENKF TFKELTFKMV DVGGQRSERK KWIHCFEGVT AIIFCVELSG YDLKLYEDNQ TSRMAESLRL FDSICNNNWF INTSLILFLN KKDLLAEKIR RIPLTICFPE YKGQNTYEEA AVYIQRQFED LNRNKETKEI YSHFTCATDT SNIQFVFDAV TDVIIQNNLK YIGLC

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:

Protease Serine 3 Human Recombinant

Protease Serine 3 (Mesotrypsin), Protease Serine 4 (Trypsin 4, Brain), Brain Trypsinogen, Mesotrypsinogen, Trypsin III, Trypsinogen IV, Trypsinogen 5, Pancreatic Trypsinogen III, MTG, TRY3, PRSS4, T9, EC 3.4.21.

Product # :

ENZ-735

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Description

PRSS3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 247 amino acids (81-304) and having a molecular mass of 26.0kDa.PRSS3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The PRSS3 solution contains 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
PRSS3 is a trypsinogen, and a member of the trypsin family of serine proteases. PRSS3 is expressed in the pancreas and brain and is unaffected by common trypsin inhibitors. It is active on peptide linkages involving the carboxyl group of lysine or arginine. PRSS3 is restricted to the locus of T cell receptor beta variable orphans on chromosome 9. 4 different isoforms encoded by 4 transcript variants were identified for this gene.
Synonyms
Protease Serine 3 (Mesotrypsin), Protease Serine 4 (Trypsin 4, Brain), Brain Trypsinogen, Mesotrypsinogen, Trypsin III, Trypsinogen IV, Trypsinogen 5, Pancreatic Trypsinogen III, MTG, TRY3, PRSS4, T9, EC 3.4.21.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSIVGGYTC EENSLPYQVS LNSGSHFCGG SLISEQWVVS AAHCYKTRIQ VRLGEHNIKV LEGNEQFINA AKIIRHPKYN RDTLDNDIML IKLSSPAVIN ARVSTISLPT APPAAGTECL ISGWGNTLSF GADYPDELKC LDAPVLTQAE CKASYPGKIT NSMFCVGFLE GGKDSCQRDS GGPVVCNGQL QGVVSWGHGC AWKNRPGVYT KVYNYVDWIK DTIAANS

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:

Mitogen-Activated Protein Kinase 12 Human Recombinant

Mitogen-activated protein kinase 12, SAPK3, ERK6, PRKM12, Extracellular signal-regulated kinase 6, Mitogen-activated protein kinase p38 gamma, Stress-activated protein kinase 3, MAP kinase 12, MAP kinase p38 gamma, MAPK 12, ERK3, p38gamma, EC 2.7.11.24, EC 2.7.11.

Product # :

PKA-015

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Description

MAPK12 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 387 amino acids (1-367 a.a.) and having a molecular mass of 44.1kDa.MAPK12 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MAPK12 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 100mM NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE analysis.

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Introduction
MAPK12 is a member of the MAP kinase family. MAPK12 acts as a signal transducer during differentiation of myoblasts to myotubes. p38 proteins utilizes magnesium as a cofactor to catalyze the ATP-dependent phosphorylation of target proteins and is produced in several regions all over the body with common expression patterns in heart.
Synonyms
Mitogen-activated protein kinase 12, SAPK3, ERK6, PRKM12, Extracellular signal-regulated kinase 6, Mitogen-activated protein kinase p38 gamma, Stress-activated protein kinase 3, MAP kinase 12, MAP kinase p38 gamma, MAPK 12, ERK3, p38gamma, EC 2.7.11.24, EC 2.7.11.
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 MSSPPPARSG FYRQEVTKTA WEVRAVYRDL QPVGSGAYGA VCSAVDGRTG AKVAIKKLYR PFQSELFAKR AYRELRLLKH MRHENVIGLL DVFTPDETLD DFTDFYLVMP FMGTDLGKLM KHEKLGEDRI QFLVYQMLKG LRYIHAAGII HRDLKPGNLA VNEDCELKIL DFGLARQADS EMTGYVVTRW YRAPEVILNW MRYTQTVDIW SVGCIMAEMI TGKTLFKGSD HLDQLKEIMK VTGTPPAEFV QRLQSDEAKN YMKGLPELEK KDFASILTNA SPLAVNLLEK MLVLDAEQRV TAGEALAHPY FESLHDTEDE PQVQKYDDSF DDVDRTLDEW KRVTYKEVLS FKPPRQLGAR VSKETPL.

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:

Magnesium-Dependent Phosphatase 1 Human Recombinant

Magnesium-dependent phosphatase 1, MGC5987, MDP-1, FN6Pase, fructosamine-6-phosphatase, SFTB3, SFTPB, MDP1.

Product # :

ENZ-044

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Description

MDP1 Human Recombinant fused with a 24 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 200 amino acids (1-176 a.a.) and having a molecular mass of 22.6kDa. The MDP1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The MDP1 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 2mM DTT and 100mM NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Magnesium-dependent phosphatase 1 (MDP1) is a memeber of the HAD-like hydrolase superfamily. MDP1 is a magnesium-dependent phosphatase which may act as a tyrosine phosphatase. MDP1 is inhibited by vanadate and zinc, and slightly by calcium.
Synonyms
Magnesium-dependent phosphatase 1, MGC5987, MDP-1, FN6Pase, fructosamine-6-phosphatase, SFTB3, SFTPB, MDP1.
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 MGSHMARLPK LAVFDLDYTL WPFWVDTHVD PPFHKSSDGT VRDRRGQDVR LYPEVPEVLK RLQSLGVPGA AASRTSEIEG ANQLLELFDL FRYFVHREIY PGSKITHFER LQQKTGIPFS QMIFFDDERR NIVDVSKLGV TCIHIQNGMN LQTLSQGLET FAKAQTGPLR SSLEESPFEA.

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:

Angiopoietin-like Protein 4 Human Recombinant

ANGPTL4, NL2, ARP4, FIAF, PGAR, HFARP, pp1158, ANGPTL2, Fasting- Induced Adipose Factor, Hepatic Fibrinogen/Angiopoietin-Related Protein, PPARG Angiopoietin-Related Protein.

Product # :

CYT-249

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Description

The ANGPTL4 Human Recombinant is manufactured with N-terminal fusion of His Tag. The Angiopoietin-like Protein 4 His -Tagged Fusion Protein is 25 kDa protein containing 204 amino acid residues of the Angiopoietin-like Protein 4 and 16 additional amino acid residues - His Tag (underlined).

Source

Escherichia Coli.

Formulation

Filtered and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
FIAF (fasting-induced adipose factor) a.k.a ANGPTL4 or PGAR or HFARP is an adipocytokine up-regulated by fasting, by peroxisome proliferator-activated receptor agonists, and by hypoxia. ANGPTL4 is found in human and mouse blood plasma both as a native protein and in a truncated form. In human white adipose tissue and SGBS adipocytes, only the native form of ANGPTL4 could be detected, whereas in mice the differentiation of mouse 3T3-L1 adipocytes is associated with the production of truncated ANGPTL4. However, the truncated ANGPTL4 is produced by human liver. In human blood plasma FIAF is mainly presented in a truncated form (FIAF-S2), whose levels treatment increases (as shown by experimental data). There is an inter individual variation in ANGPTL4 levels of both the truncated and the native form, however those levels were not influenced by prolonged semistarvation and are not associated with body mass index.
Synonyms
ANGPTL4, NL2, ARP4, FIAF, PGAR, HFARP, pp1158, ANGPTL2, Fasting- Induced Adipose Factor, Hepatic Fibrinogen/Angiopoietin-Related Protein, PPARG Angiopoietin-Related Protein.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized Angiopoietin-like Protein 4 Human recombinant at -20°C. Aliquot the ANGPTL4 after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted ANGPTL4 can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
Add 0.1M Acetate buffer pH4 and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this antigen is limited.
Amino Acid Sequence
MRGSHHHHHH GMASHMGPVQ SKSPRFASWD EMNVLAHGLL QLGQGLREHA ERTRSQLSAL ERRLSACGSA CQGTEGSTDL PLAPESRVDP EVLHSLQTQL KAQNSRIQQL FHKVAQQQRH LEKQHLRIQH LQSQFGLLDH KHLDHEVAKP ARRKRLPEMA QPVDPAHNVS RLHRLPRDCQ ELFQVGERQS GLFEIQPQGS PPFLVNCKMT SDGGWTVIQR.
Background
Angiopoietin-like Protein 4 Human Recombinant: A Promising Therapeutic Approach for Metabolic Disorders
Abstract:

Angiopoietin-like protein 4 (ANGPTL4) is a multifunctional protein involved in the regulation of lipid metabolism and energy homeostasis. It has emerged as a potential therapeutic target for metabolic disorders, including obesity, dyslipidemia, and insulin resistance. The availability of human recombinant ANGPTL4 protein has provided researchers with a valuable tool to investigate its biological functions and explore its therapeutic potential. This concise review provides an overview of the role of ANGPTL4 in metabolic regulation and discusses the potential of ANGPTL4 human recombinant protein as a therapeutic intervention.
Introduction:

Metabolic disorders are a global health challenge with significant implications for cardiovascular health. ANGPTL4, a member of the angiopoietin-like protein family, has gained attention for its role in lipid metabolism and energy balance. ANGPTL4 influences the uptake, storage, and utilization of lipids, as well as glucose metabolism, making it an attractive target for therapeutic interventions.
Mechanisms of ANGPTL4 Action:

ANGPTL4 exerts its effects through multiple mechanisms. It inhibits lipoprotein lipase (LPL) activity, reducing the hydrolysis of triglycerides and leading to elevated plasma triglyceride levels. ANGPTL4 also promotes adipose tissue lipolysis, facilitating the release of fatty acids for energy utilization. Moreover, ANGPTL4 affects glucose metabolism by modulating insulin signaling and glucose uptake in various tissues.
Role of ANGPTL4 in Metabolic Regulation:

ANGPTL4 plays a critical role in lipid and glucose metabolism. It regulates plasma lipid levels by modulating LPL activity and lipid uptake in adipose tissue and skeletal muscle. ANGPTL4 also influences energy homeostasis by promoting lipid mobilization from adipocytes and regulating fatty acid oxidation. Additionally, ANGPTL4 impacts glucose metabolism by modulating insulin sensitivity and glucose uptake in skeletal muscle and adipose tissue.
Therapeutic Potential of ANGPTL4 Human Recombinant Protein:

The availability of ANGPTL4 human recombinant protein opens new avenues for therapeutic interventions targeting metabolic disorders. Administration of ANGPTL4 recombinant protein or modulation of ANGPTL4 activity offers potential strategies to improve lipid profiles, reduce adiposity, and enhance insulin sensitivity. Preclinical studies have shown promising results, demonstrating the potential of ANGPTL4 as a therapeutic target for metabolic disorders.
Conclusion:

ANGPTL4 represents a promising target for therapeutic interventions in metabolic disorders. Its involvement in the regulation of lipid and glucose metabolism makes it an attractive candidate for the development of novel treatment approaches. The availability of ANGPTL4 human recombinant protein enables further exploration of its therapeutic potential and may contribute to the development of effective interventions for metabolic disorders.
What is the molecular weight/Mw of ANGPTL4 Protein?
ANGPTL4 Protein has a total Mw of 25kDa.

What is the source or expression system of ANGPTL4 Protein?
Escherichia Coli.

What is the Purity of ANGPTL4 Protein?
ANGPTL4 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of ANGPTL4 Protein?
The biological functionality of ANGPTL4 Protein will be determined in the future.

What is the amino acid sequence of ANGPTL4 Protein?
MRGSHHHHHH GMASHMGPVQ SKSPRFASWD EMNVLAHGLL QLGQGLREHA ERTRSQLSAL ERRLSACGSA CQGTEGSTDL PLAPESRVDP EVLHSLQTQL KAQNSRIQQL FHKVAQQQRH LEKQHLRIQH LQSQFGLLDH KHLDHEVAKP ARRKRLPEMA QPVDPAHNVS RLHRLPRDCQ ELFQVGERQS GLFEIQPQGS PPFLVNCKMT SDGGWTVIQR.

What applications can ANGPTL4 Protein be used in?
ANGPTL4 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for ANGPTL4 Protein?
The endotoxin level is minimal, ANGPTL4 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:

RAS-like, Estrogen-Regulated, Growth Inhibitor Human Recombinant

Ras-related and estrogen-regulated growth inhibitor, RERG, MGC15754.

Product # :

PRO-106

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Description

RERG 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 219 amino acids (1-199 a.a.) and having a molecular mass of 24.7kDa (Molecular size on SDS-PAGE will appear higher). The RERG is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The RERG solution (0.25 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 50% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
RERG is a 199 amino acid protein which localizes in the cytoplasm and is a member of the Ras subfamily of small GTPases. RERG is expressed in the pancreas, liver, skin, lung, brain, kidney and heart tissue. RERG is a vital mediator of diverse cell signaling pathways, including those leading to cell proliferation, cytoskeletal organization and secretion.
Synonyms
Ras-related and estrogen-regulated growth inhibitor, RERG, MGC15754.
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 MAKSAEVKLA IFGRAGVGKS ALVVRFLTKR FIWEYDPTLE STYRHQATID DEVVSMEILD TAGQEDTIQR EGHMRWGEGF VLVYDITDRG SFEEVLPLKN ILDEIKKPKN VTLILVGNKA DLDHSRQVST EEGEKLATEL ACAFYECSAC TGEGNITEIF YELCREVRRR RMVQGKTRRR SSTTHVKQAI NKMLTKISS.

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Description:

Axin Interactor Dorsalization Associated Human Recombinant

C1orf80, RP11-378J18.7, Axin interactor, dorsalization-associated protein, Axin interaction partner and dorsalization antagonist, AIDA.

Product # :

PRO-1370

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Description

AIDA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 329 amino acids (1-306 a.a) and having a molecular mass of 37.4kDa. AIDA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

AIDA protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.2M NaCl and 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Axin interactor, dorsalization-associated (AIDA) operates as a ventralizing factor during embryogenesis. AIDA inhibits axin-mediated JNK activation by binding axin and disrupting axin homodimerization. That in turn antagonizes a Wnt/beta-catenin-independent dorsalization pathway activated by AXIN/JNK-signaling.
Synonyms
C1orf80, RP11-378J18.7, Axin interactor, dorsalization-associated protein, Axin interaction partner and dorsalization antagonist, AIDA.
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 MGSMSEVTRS LLQRWGASFR RGADFDSWGQ LVEAIDEYQI LARHLQKEAQ AQHNNSEFTE EQKKTIGKIA TCLELRSAAL QSTQSQEEFK LEDLKKLEPI LKNILTYNKE FPFDVQPVPL RRILAPGEEE NLEFEEDEEE GGAGAGSPDS FPARVPGTLL PRLPSEPGMT LLTIRIEKIG LKDAGQCIDP YITVSVKDLN GIDLTPVQDT PVASRKEDTY VHFNVDIELQ KHVEKLTKGA AIFFEFKHYK PKKRFTSTKC FAFMEMDEIK PGPIVIELYK KPTDFKRKKL QLLTKKPLYL HLHQTLHKE.

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Description:

Transforming Growth Factor Beta Receptor 1 Human Recombinant, Active

TGFBR1, AAT5, ACVRLK4, ALK-5, ALK5, ESS1, LDS1, LDS1A, LDS2A, MSSE, SKR4, tbetaR-I, TGFR-1.

Product # :

PKA-135

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Description

TGFBR1 produced in Sf9 insect cells is a single, glycosylated polypeptide chain containing 342 amino acids (27-126a.a.) and having a molecular mass of 38kDa. TGFBR1 is expressed with 242 amino acid hIgG-His-Tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

TGFBR1 protein solution (0.5mg/ml) Phosphate Buffered Saline (pH 7.4) containing 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

≤ 2 ug/ml, measured by its binding ability in a functional ELISA with Mouse CD105.

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Synonyms
TGFBR1, AAT5, ACVRLK4, ALK-5, ALK5, ESS1, LDS1, LDS1A, LDS2A, MSSE, SKR4, tbetaR-I, TGFR-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
ADLLLPGATA LQCFCHLCTK DNFTCVTDGL CFVSVTETTD KVIHNSMCIA EIDLIPRDRP FVCAPSSKTG SVTTTYCCNQ DHCNKIELPT TVKSSPGLGP VELVEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL
PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.
Background
Transforming Growth Factor Beta Receptor 1 (TGFBR1), a transmembrane protein crucial in the TGF-β signaling pathway, holds a paramount position in regulating diverse cellular processes. Its intricate involvement in development, immune responses, tissue homeostasis, and disease has elevated TGFBR1 to a central role in biology and medicine. This research embarks on a comprehensive exploration of the TGFBR1 protein, unraveling its structural complexities, signaling mechanisms, and its far-reaching implications in various physiological and pathological contexts. By dissecting the intricacies of TGFBR1, scientists aim to decode the fundamental cellular processes it governs and explore potential therapeutic avenues in the domains of cancer, fibrosis, and immunology.
Structural Complexity of TGFBR1:
TGFBR1 is a serine/threonine kinase receptor with an extracellular ligand-binding domain, a transmembrane domain, and an intracellular kinase domain. Its structure allows it to interact with TGF-β ligands and initiate downstream signaling cascades. Understanding the three-dimensional architecture of TGFBR1 is pivotal for deciphering its interactions with ligands, co-receptors, and intracellular signaling partners, shedding light on the molecular intricacies of its function.
Signaling Pathways and Physiological Functions:
Upon ligand binding, TGFBR1 phosphorylates downstream effectors, regulating processes like cell proliferation, differentiation, apoptosis, and immune responses. TGF-β signaling mediated by TGFBR1 is vital in embryogenesis, tissue repair, and immune tolerance. Dysregulation of this pathway is implicated in numerous diseases, including cancer, fibrosis, and autoimmune disorders, underscoring the significance of TGFBR1 in maintaining cellular and tissue homeostasis.
TGFBR1 in Cancer Biology:
TGFBR1's dual role as a tumor suppressor and a promoter of cancer progression reflects its complexity in cancer biology. In early stages, TGFBR1 signaling suppresses cell growth and promotes apoptosis, acting as a defense against tumorigenesis. However, in advanced stages, cancer cells exploit TGFBR1 signaling to facilitate invasion, metastasis, and immune evasion. Understanding the context-dependent nature of TGFBR1's functions in cancer is pivotal for developing targeted therapies.
Targeting TGFBR1 in Therapeutics:
Given its critical roles in various diseases, TGFBR1 has emerged as an attractive target for therapeutic interventions. In cancer, efforts are underway to develop small molecule inhibitors and monoclonal antibodies that modulate TGFBR1 signaling, aiming to curb tumor progression. Additionally, in fibrotic disorders, targeting TGFBR1 offers hope for halting the pathological tissue remodeling characteristic of these diseases, providing potential treatments for conditions such as pulmonary fibrosis and liver cirrhosis.
TGFBR1 Protein, with its intricate signaling mechanisms and diverse physiological roles, stands at the crossroads of fundamental cellular processes and disease pathogenesis. Its involvement in development, immune regulation, cancer, and tissue homeostasis underscores its significance in biology and medicine. As researchers delve deeper into the complexities of TGFBR1, they pave the way for innovative therapies and a deeper understanding of diseases, ultimately shaping the future of healthcare and scientific exploration. This research not only illuminates the pivotal role of TGFBR1 but also holds the promise of transformative advancements in medicine and our understanding of cellular signaling pathways.

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:

Proteasome Beta Type 10 Human Recombinant

Proteasome subunit beta type-10, Low molecular mass protein 10, Macropain subunit MECl-1, Multicatalytic endopeptidase complex subunit MECl-1, Proteasome MECl-1, Proteasome subunit beta-2i, PSMB10, LMP10, MECL1, beta2i, MGC1665, FLJ00366.

Product # :

PRO-931

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Description

PSMB10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 255 amino acids (40-273 a.a.) and having a molecular mass of 26.9kDa.PSMB10 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

PSMB10 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 40% glycerol and 0.1M NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
PSMB10 is a member of the proteasome B-type family (T1B family) which is a 20S core beta subunit. The proteasome is a multicatalytic proteinase complex with an extremely ordered ring-shaped 20S core structure. This core structure is comprised of four rings of 28 non-identical subunits; two rings are composed of seven alpha subunits and two rings are composed of seven beta subunits. Proteasomes are circulated in eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. A crucial function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. PSMB10 gene expression is induced by INFg, and it replaces catalytic subunit 2 (proteasome beta 7 subunit) in the immunoproteasome.
Synonyms
Proteasome subunit beta type-10, Low molecular mass protein 10, Macropain subunit MECl-1, Multicatalytic endopeptidase complex subunit MECl-1, Proteasome MECl-1, Proteasome subunit beta-2i, PSMB10, LMP10, MECL1, beta2i, MGC1665, FLJ00366.
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 MTTIAGLVFQ DGVILGADTR ATNDSVVADK SCEKIHFIAP KIYCCGAGVA ADAEMTTRMV ASKMELHALS TGREPRVATV TRILRQTLFR YQGHVGASLI VGGVDLTGPQ LYGVHPHGSY SRLPFTALGS GQDAALAVLE DRFQPNMTLE AAQGLLVEAV
TAGILGDLGS GGNVDACVIT KTGAKLLRTL SSPTEPVKRS GRYHFVPGTT AVLTQTVKPL TLELVEETVQ AMEVE.

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Description:

Neuralized Homolog 2 Human Recombinant

800x600 800x600 800x600 neuralized homolog 2, C20orf163, OZZ, Ozz-E3, Neuralized-like protein 2, Neuralized Homolog 2, NEURL2. Normal 0 false false false EN-US X-NONE HE MicrosoftInternetExplorer4 /* Style Definitions */ table.MsoNormalTable {mso-style-name:"Table Normal"; mso-tstyle-rowband-size:0; mso-tstyle-colband-size:0; mso-style-noshow:yes; mso-style-priority:99; mso-style-parent:""; mso-padding-alt:0cm 5.4pt 0cm 5.4pt; mso-para-margin:0cm; mso-para-margin-bottom:.0001pt; mso-pagination:widow-orphan; font-size:10.0pt; font-family:"Calibri","sans-serif";}

Product # :

PRO-1678

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Description

NEURL2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 308 amino acids (1-285) and having a molecular mass of 34.1 kDa.NEURL2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The NEURL2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Neuralized Homolog 2 (NEURL2) takes part in the process of myofiber differentiation and maturation. NEURL2 is probable substrate-recognition component of a SCF-like ECS E3 ubiquitin-protein ligase complex, which mediates the ubiquitination of proteins. NEURL2 contributes to catalysis through recognition and positioning of the substrate and the ubiquitin-conjugating enzyme. NEURL2 regulates the ubiquitin-mediated degradation of beta-catenin during myogenesis.
Synonyms
neuralized homolog 2, C20orf163, OZZ, Ozz-E3, Neuralized-like protein 2, Neuralized Homolog 2, NEURL2.
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 MGSMAAASEP VDSGALWGLE RPEPPPTRFH RVHGANIRVD PSGTRATRVE SFAHGVCFSR EPLAPGQVFL VEIEEKELGW CGHLRLGLTA LDPASLAPVP EFSLPDLVNL GHTWVFAITR HHNRVPREGR PEAEAAAPSR PPTLLVEPYL RIEQFRIPRD
RLVGRSRPGL YSHLLDQLYE LNVLPPTARR SRLGVLFCPR PDGTADMHII INGEDMGPSA RGLPAAQPLY AVVDVFASTK SVRLVQLEYG LPSLQTLCRL VIQRSMVHRL AIDGLHLPKE LKDFCKYE.

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:

VEGF Co-regulated Chemokine 1 Rat Recombinant

Protein Cxcl17, Cxcl17, RGD1304717, C-X-C motif chemokine 17, VEGF co-regulated chemokine 1, Vcc1, VCC-1.

Product # :

CHM-281

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Description

CXCL17 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 97 amino acids and having a molecular mass of 11.5kDa.The CXCL17 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CXCL17 protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, 300mM NaCl, pH 7.4.

Purity

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

Biological Activity

Measured by its ability to induce VEGF expression in mouse endothelial cells. The ED₅₀ for this effect is typically 1-5 µg/ml.

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Introduction
Dendritic cell and monocyte chemokinelike protein (DMC/CXCL17/VEGF-correlated chemokine 1/VCC1), is a secreted molecule with a size and predicted 3-dimensional folding pattern similar to that of chemokines CXCL8/IL8 and CXCL14/BRAK. CXCL17 is constitutively generated by airway and intestinal epithelium. CXCL17 induces the chemotaxis of quiescent, but not LPS-activated peripheral blood monocytes and dendritic cells, and it also binds these cells specifically. The expression of CXCL17 is increased in endothelial cells when they are induced to form tubes in vitro. CXCL17, CXCL1/GRO and CXCL8/IL8 which have roles in angiogenesis, show significantly correlated expression with that of VEGF in primary lung, breast and esophageal tumors. Therefore, CXCL17 is suggested to have a role in tumor angiogenesis. The mature Rat CXCL17 shares 82%, 71% amino acid sequence identity with mouse, human CXCL17, respectively.
Synonyms
Protein Cxcl17, Cxcl17, RGD1304717, C-X-C motif chemokine 17, VEGF co-regulated chemokine 1, Vcc1, VCC-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CXCL17 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL17 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 CXCL17 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SPNQEVARHH GDQHQAPRRW LWEGGQECDC KDWSLRVSKR KTTAVLEPPR KQCPCDHVKG SEKKNRRQKH HRKSQRPSRT CQQFLKRCQL ASFTLPL.
Background
What is the molecular weight/Mw of CXCL17 RAT Protein?
CXCL17 RAT Protein has a total Mw of 11.5kDa.

What is the source or expression system of CXCL17 RAT Protein?
Escherichia Coli.

What is the Purity of CXCL17 RAT Protein?
CXCL17 RAT Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL17 RAT Protein?
Measured by its ability to induce VEGF expression in mouse endothelial cells. The ED50 for this effect is typically 1-5 µg/ml.

What is the amino acid sequence of CXCL17 RAT Protein?
SPNQEVARHH GDQHQAPRRW LWEGGQECDC KDWSLRVSKR KTTAVLEPPR KQCPCDHVKG SEKKNRRQKH HRKSQRPSRT CQQFLKRCQL ASFTLPL.

What applications can CXCL17 RAT Protein be used in?
CXCL17 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL17 RAT Protein?
The endotoxin level is minimal, CXCL17 RAT Protein was purified using conventional chromatography techniques.

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

Description:

PLAUR Human Recombinant

PLAUR, Monocyte Activation Antigen Mo3, U-PAR, UPAR, U-Plasminogen Activator Receptor Form 2, CD87 Antigen , CD87, URKR, MO3.

Product # :

PRO-2340

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Description

PLAUR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 291 amino acids (23-305 a.a.) and having a molecular mass of 32.5kDa (Molecular size on SDS-PAGE will appear at approximately 40-57 kDa).PLAUR is fused to a 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
PLAUR is one of 2 activators which convert the extracellular zymogen plasminogen to plasmin, a serine protease involved in a various normal and pathological processes that require cell migration and/or tissue destruction. PLAUR protein is synthesized and released from cells as a single-chain proenzyme with narrow enzymatic activity and is converted to an active two-chain disulfide-linked active enzyme by plasmin and other specific proteinases.
Synonyms
PLAUR, Monocyte Activation Antigen Mo3, U-PAR, UPAR, U-Plasminogen Activator Receptor Form 2, CD87 Antigen , CD87, URKR, MO3.
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
LRCMQCKTNG DCRVEECALG QDLCRTTIVR LWEEGEELEL VEKSCTHSEK TNRTLSYRTG LKITSLTEVV CGLDLCNQGN SGRAVTYSRS RYLECISCGS SDMSCERGRH QSLQCRSPEE QCLDVVTHWI QEGEEGRPKD DRHLRGCGYL PGCPGSNGFH NNDTFHFLKC CNTTKCNEGP ILELENLPQN GRQCYSCKGN STHGCSSEET FLIDCRGPMN QCLVATGTHE PKNQSYMVRG CATASMCQHA HLGDAFSMNH IDVSCCTKSG CNHPDLDVQY RSGLEHHHHH H.

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

Description:

Tumor Necrosis Factor Receptor Type 2 Human Recombinant, His Tag

Tumor necrosis factor receptor superfamily member 1B, Tumor necrosis factor receptor 2, Tumor necrosis factor receptor type II, p75, p80 TNF-alpha receptor, CD120b, Etanercept, TNF-R2, TNF-RII, TNFR-II, TNFRSF1B, TNFBR, TNFR2, TBPII, TNFR2, TNFR1B, TNFR80, TNF-R75, p75TNFR, TNF-R-II.

Product # :

CYT-674

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Description

TNFR2 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 184 amino acids fragment (23-206) having a molecular weight of 24.45kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The TNFR2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TNFR2 protein is supplied in 20mM Tris HCl pH-8, 5mM EDTA and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
TNFR2 belongs to the TNF-receptor superfamily. TNFR2 is receptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. TNFR2 mediates the majority of the metabolic effects of TNF-alpha. In addition, knockout studies in mice propose a role for TNFR2 in protecting neurons from apoptosis by stimulating antioxidative pathways. TNFR2 expression might have a significant role in the angiogenesis, tumor cell proliferation and metastasis of Invasive micropapillary carcinoma of the breast.
There are 2 types of soluble TNF receptors: sTNFR-I and sTNFR-II, which act to neutralize the biological activities of TNF alpha and TNF beta. The levels of these soluble receptors seem to increase as a result of shedding of the extracellular domains of the membrane bound receptors. High levels of soluble TNF receptors are found in the amniotic fluid of pregnant women. TNFR2 and TNFR1 form a heterocomplex which mediates the recruitment of 2 anti-apoptotic proteins, c-IAP1 and c-IAP2, which possess E3 ubiquitin ligase activity. IAPs’ function in TNF-receptor signaling is unknown; nevertheless, c-IAP1 is believed to potentiate TNF-induced apoptosis by the ubiquitination and degradation of TNF-receptor-associated factor 2, which mediates anti-apoptotic signals. Oxidative stress promotes TNFR1 and TNFR2 self-interaction, ligand-independent and enhanced ligand-dependent TNF signaling. TNF-a, TNFR1 and TNFR2 have roles in cellular differentiation. TNFR1 and TNFR2 function in cell type-specific renal injury.
Synonyms
Tumor necrosis factor receptor superfamily member 1B, Tumor necrosis factor receptor 2, Tumor necrosis factor receptor type II, p75, p80 TNF-alpha receptor, CD120b, Etanercept, TNF-R2, TNF-RII, TNFR-II, TNFRSF1B, TNFBR, TNFR2, TBPII, TNFR2, TNFR1B, TNFR80, TNF-R75, p75TNFR, TNF-R-II.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
Amino Acid Sequence
LPAQVAFTPYAPEPGSTCRLREYYDQTAQMCCSKCSPGQHAKVFCTKTSDTVCDSCEDSTYTQLWNWV
PECLSCGSRCSSDQVETQACTREQNRICTCRPGWYCALSKQEGCRLCAPLRKCRPGFGVARPGTETSD
VVCKPCAPGTFSNTTSSTDICRPHQICNVVAIPGNASMDAVCTSTSPT.

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:

Myostatin Polyclonal Rabbit Anti Human Antibody

GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.

Product # :

ANT-041

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Shipping Method :

Shipped at Room temp

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Formulation

Lyophilized from 1mg/ml solution in 0.2µm sterile filtered solution in phosphate buffered saline.

Purity

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

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Introduction
GDF8 is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. This gene is thought to encode a secreted protein which negatively regulates skeletal muscle growth.
Synonyms
GDF-8, MSTN, Growth Differentiation Factor 8, MSTN Muscle Hypertrophy.
Stability
Store at 4°C. For long term storage freezes in working aliquots at -20°C. Repeated freezing and thawing is not recommended.
Solubility
Reconstitute with H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.Human Myostatin
Ig Subclass
Rabbit IgG
Applications
To detect Human Myostatin by WB analysis this IgG can be used in a dilution of 1/500.
To optimal usage we suggest overnight incubation.
Antigen Amino Acid Sequence
HHHHHHDFGL DCDEHSTESR CCRYPLTVDF EAFGWDWIIA PKRYKANYCS GECEFVFLQKYPHTHLVHQA NPRGSAGPCC TPTKMSPINM LYFNGKEQII YGKIPAMVVD RCGCS
Type
Polyclonal Rabbit Antibody.
Purification Method
Purified IgG prepared by affinity chromatography on protein G.

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:

Neutrophil Gelatinase Associated Lipocalin/Lipocalin-2 Human Recombinant, His Tag

Neutrophil gelatinase-associated lipocalin, NGAL, p25, 25 kDa alpha-2-microglobulin-related subunit of MMP-9, Lipocalin-2, Oncogene 24p3, LCN2.

Product # :

ENZ-297

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Description

Neutrophil Gelatinase Associated Lipocalin Human Recombinant is expressed in E. coli having a molecular weight of 28.1 kDa fused to an amino terminal hexahistidine tag.The LCN2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lipocalin-2 is supplied in PBS, 50% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.
Single band on Western Blot.

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Introduction
Recombinant Human Lipocalin-2 also called Neutrophil Gelatinase Associated Lipocalin (NGAL) belongs to a family of lipocans which include 25 proteins (including a1-microglobulin and b-lactoglobulin), which are characterized by their ability to bind small lipophilic substances in their hydrophobic core.
They thereby serve as transporters of substances like retinal, biliverdins & prostaglandins. There are indications that NGAL is involved in modulation of the inflammatory response and is found in the plasma of patients after stroke.
Synonyms
Neutrophil gelatinase-associated lipocalin, NGAL, p25, 25 kDa alpha-2-microglobulin-related subunit of MMP-9, Lipocalin-2, Oncogene 24p3, LCN2.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

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:

Enteropeptidase/ Enterokinase, Light Chain Human Recombinant

Enteropeptidase, EC 3.4.21.9, Enterokinase, Serine protease 7, ENTK,TMPRSS15, MGC133046, Transmembrane Protease Serine 15.

Product # :

ENZ-260

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Description

Enterokinase Human produced in E.Coli cells is a single, non-glycosylated polypeptide chain containing 237 amino acids (785-1019aa ) and having a molecular mass of 26.4kDa. Enterokinase is purified by proprietary chromatographic techniques

Source

Escherichia Coli.

Formulation

Enterokinase 1mg/ml is supplied in 20mM Tris-HCl, pH 8.0, and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Enteropeptidase or enterokinase is an enzymeinvolved in human digestion. It is produced by cells in the duodenum wall, and is secreted from duodenum's glands, the crypts of Lieberk?hn, whenever ingested food enters the duodenum from the stomach. Enteropeptidase has the critical job of turning trypsinogen(a zymogen) to trypsin, indirectly activating a number of pancreaticdigestive enzymes.
Enteropeptidase is a serine proteaseenzyme(EC3.4.21.9). Enteropeptidase is a part of the Chymotrypsin-clan of serine proteases, and is structurally similar to these proteins.
Synonyms
Enteropeptidase, EC 3.4.21.9, Enterokinase, Serine protease 7, ENTK,TMPRSS15, MGC133046, Transmembrane Protease Serine 15.
Physical Appearance
Liquid 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
MAIVGGSNAK EGAWPWVVGL YYGGRLLCGA SLVSSDWLVS AAHCVYGRNL EPSKWTAILG LHMKSNLTSP QTVPRLIDEI VINPHYNRRR KDNDIAMMHL EFKVNYTDYI QPICLPEENQ VFPPGRNCSI AGWGTVVYQG TTANILQEAD VPLLSNERCQ QQMPEYNITE NMICAGYEEG GIDSCQGDSG GPLMCQENNR WFLAGVTSFG YKCALPNRPG VYARVSRFTE WIQSFLH

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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